Evaluation of Three Quantitative Anti-SARS-CoV-2 Antibody Immunoassays Sabine Chapuy-Regaud et al. Microbiol Spectr. 2021. Free PMC article Abstract The severe acute respiratory syndrome coronavirus 2 SARS-CoV-2 emerged in December 2019 and caused a dramatic pandemic. Serological assays are used to check for immunization and assess herd immunity. We evaluated commercially available assays designed to quantify antibodies directed to the SARS-CoV-2 Spike S antigen, either total Wantaï SARS-CoV-2 Ab ELISA or IgG SARS-CoV-2 IgG II Quant on Alinity, Abbott, and Liaison SARS-CoV-2 TrimericS IgG, Diasorin. The specificities of the Wantaï, Alinity, and Liaison assays were evaluated using 100 prepandemic sera and were 98, 99, and 97%, respectively. The sensitivities of all three were around 100% when tested on 35 samples taken 15 to 35 days postinfection. They were less sensitive for 150 sera from late infections >180 days. Using the first WHO international standard NIBSC, we showed that the Wantai results were concordant with the NIBSC values, while Liaison and Alinity showed a proportional bias of and 7, respectively. The results of the 3 immunoassays were significantly globally pairwise correlated and for late infection sera P < They were correlated for recent infection sera measured with Alinity and Liaison P < However, the Wantai results of recent infections were not correlated with those from Alinity or Liaison. All the immunoassay results were significantly correlated with the neutralizing antibody titers obtained using a live virus neutralization assay with the SARS-CoV-2 strain. These assays will be useful once the protective anti-SARS-CoV-2 antibody titer has been determined. IMPORTANCE Standardization and correlation with virus neutralization assays are critical points to compare the performance of serological assays designed to quantify anti-SARS-CoV-2 antibodies in order to identify their optimal use. We have evaluated three serological immunoassays based on the virus spike antigen that detect anti-SARS-CoV-2 antibodies a microplate assay and two chemiluminescent assays performed with Alinity Abbott and Liaison Diasorin analysers. We used an in-house live virus neutralization assay and the first WHO international standard to assess the comparison. This study could be useful to determine guidelines on the use of serological results to manage vaccination and treatment with convalescent plasma or monoclonal antibodies. Keywords COVID; SARS-CoV-2; binding antibodies; immunoassay; neutralizing antibodies. Conflict of interest statement The authors declare no conflict of interest. Figures FIG 1 Distribution of the results. A Wantaï, B Liaison, and C Alinity assays according to patient groups. Black lines = median of each group. Red lines = manufacturer’s negative/positive threshold. Zero 0 values in the Liaison negative group n = 92, the Liaison late infection group n = 15, the Alinity negative group n = 14, and the Alinity late infection group n = 7 are not shown. FIG 2 ROC curves for Wantaï black line, Liaison green line and Alinity red line. Gray line y = x. The AUROCs were Wantaï 95% CI to Liaison 95% CI to and Alinity 95% CI to indicating their capacity to accurately detect anti-SARS-CoV-2 antibodies. FIG 3 Quantification of anti-SARS-CoV-2 antibodies relative to the NIBSC international standard. Serial dilutions of the NIBSC 20/136 standard were assayed with the A Wantaï, B Liaison, and C Alinity assay. Neutralizing antibodies NAb were also determined with a live method D. The black line represents the regression line and the dashed lines its 95% CI. The dashed red line represents the y = x line. AU arbitrary units. BAU binding antibody unit. The equations were y = x − slope 95% CI to y-intercept 95% CI − to for Wantaï; y = x − slope 95% CI to y-intercept 95% CI − to for Liaison; y = x - slope 95% CI to y-intercept 95% CI − to for Alinity and y = x + slope 95% CI to y-intercept 95% CI − to for NAb titers. FIG 4 Correlation between the immunoassay results. Pairwise distribution of the Wantaï, Liaison, and Alinity assays values for all positive results A to C, recent infections D to F, and late infections G to I. When the Spearman rank coefficient r indicated a significant correlation, the regression line was drawn. Dashed lines 95% CI limits. FIG 5 Immunoassays results and neutralizing antibody titers. Distribution of the Wantaï, Liaison, and Alinity assay values and the NAb titers for all positive results A to C The NAb titers were determined in a live virus neutralization assay using the B strain. Spearman’s rank coefficients r and their P value are indicated. The box extends from the 25th to 75th percentiles and whiskers from minimal to maximal values. Similar articles Performance evaluation of three automated quantitative immunoassays and their correlation with a surrogate virus neutralization test in coronavirus disease 19 patients and pre-pandemic controls. Jung K, Shin S, Nam M, Hong YJ, Roh EY, Park KU, Song EY. Jung K, et al. J Clin Lab Anal. 2021 Sep;359e23921. doi Epub 2021 Aug 8. J Clin Lab Anal. 2021. PMID 34369009 Free PMC article. Inference of SARS-CoV-2 spike-binding neutralizing antibody titers in sera from hospitalized COVID-19 patients by using commercial enzyme and chemiluminescent immunoassays. Valdivia A, Torres I, Latorre V, Francés-Gómez C, Albert E, Gozalbo-Rovira R, Alcaraz MJ, Buesa J, Rodríguez-Díaz J, Geller R, Navarro D. Valdivia A, et al. Eur J Clin Microbiol Infect Dis. 2021 Mar;403485-494. doi Epub 2021 Jan 6. Eur J Clin Microbiol Infect Dis. 2021. PMID 33404891 Free PMC article. Serological Assays for Assessing Postvaccination SARS-CoV-2 Antibody Response. Mahmoud SA, Ganesan S, Naik S, Bissar S, Zamel IA, Warren KN, Zaher WA, Khan G. Mahmoud SA, et al. Microbiol Spectr. 2021 Oct 31;92e0073321. doi Epub 2021 Sep 29. Microbiol Spectr. 2021. PMID 34585943 Free PMC article. Overview of Neutralization Assays and International Standard for Detecting SARS-CoV-2 Neutralizing Antibody. Liu KT, Han YJ, Wu GH, Huang KA, Huang PN. Liu KT, et al. Viruses. 2022 Jul 18;1471560. doi Viruses. 2022. PMID 35891540 Free PMC article. Review. Recent Developments in SARS-CoV-2 Neutralizing Antibody Detection Methods. Banga Ndzouboukou JL, Zhang YD, Fan XL. Banga Ndzouboukou JL, et al. Curr Med Sci. 2021 Dec;4161052-1064. doi Epub 2021 Dec 21. Curr Med Sci. 2021. PMID 34935114 Free PMC article. Review. Cited by Diagnostic performance of four lateral flow immunoassays for COVID-19 antibodies in Peruvian population. Calderon-Flores R, Caceres-Cardenas G, Alí K, De Vos M, Emperador D, Cáceres T, Eca A, Villa-Castillo L, Albertini A, Sacks JA, Ugarte-Gil C. Calderon-Flores R, et al. PLOS Glob Public Health. 2023 Jun 2;36e0001555. doi eCollection 2023. PLOS Glob Public Health. 2023. PMID 37267241 Free PMC article. Correlation of Postvaccination Fever With Specific Antibody Response to Severe Acute Respiratory Syndrome Coronavirus 2 BNT162b2 Booster and No Significant Influence of Antipyretic Medication. Tani N, Ikematsu H, Goto T, Gondo K, Inoue T, Yanagihara Y, Kurata Y, Oishi R, Minami J, Onozawa K, Nagano S, Kuwano H, Akashi K, Shimono N, Chong Y. Tani N, et al. Open Forum Infect Dis. 2022 Sep 23;910ofac493. doi eCollection 2022 Oct. Open Forum Infect Dis. 2022. PMID 36267253 Free PMC article. Current immunoassays and detection of antibodies elicited by Omicron SARS-CoV-2 infection. Migueres M, Chapuy-Regaud S, Miédougé M, Jamme T, Lougarre C, Da Silva I, Pucelle M, Staes L, Porcheron M, Diméglio C, Izopet J. Migueres M, et al. J Med Virol. 2023 Jan;951e28200. doi Epub 2022 Oct 17. J Med Virol. 2023. PMID 36207814 Free PMC article. SARS-CoV-2 anti-spike antibodies after a fourth dose of COVID-19 vaccine in adult solid-organ transplant recipients. Perrier Q, Lupo J, Gerster T, Augier C, Falque L, Rostaing L, Pelletier L, Bedouch P, Blanc M, Saint-Raymond C, Boignard A, Bonadona A, Noble J, Epaulard O. Perrier Q, et al. Vaccine. 2022 Oct 19;40446404-6411. doi Epub 2022 Sep 6. Vaccine. 2022. PMID 36184404 Free PMC article. Can the COVID-19 Pandemic Improve the Management of Solid Organ Transplant Recipients? Del Bello A, Marion O, Izopet J, Kamar N. Del Bello A, et al. Viruses. 2022 Aug 24;1491860. doi Viruses. 2022. PMID 36146666 Free PMC article. Review. 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Everyonewho has symptoms that are consistent with COVID-19 and people with known high-risk exposures to SARS-CoV-2 should be tested for SARS-CoV-2 infection. Such testing should employ either a nucleic acid amplification test (NAAT) or an antigen test to detect SARS-CoV-2. Testing may also be used for screening, determining the length of a

bySevere Acute Respiratory Syndrome-Corona Virus-2 (SARS-CoV-2). The clinical manifestations caused by this virus also vary. Starting from asymptomatic and symptomatic or symptomatic. With the incubation period required by SARS-CoV-2 and asymptomatic cases that make the spread of this virus difficult to detect.

Brief Communication Published 29 April 2020 Bai-Zhong Liu2 na1, Hai-Jun Deng ORCID na1, Gui-Cheng Wu3,4 na1, Kun Deng5 na1, Yao-Kai Chen6 na1, Pu Liao7, Jing-Fu Qiu8, Yong Lin ORCID Xue-Fei Cai1, De-Qiang Wang1, Yuan Hu1, Ji-Hua Ren1, Ni Tang1, Yin-Yin Xu2, Li-Hua Yu2, Zhan Mo2, Fang Gong2, Xiao-Li Zhang2, Wen-Guang Tian2, Li Hu2, Xian-Xiang Zhang3,4, Jiang-Lin Xiang3,4, Hong-Xin Du3,4, Hua-Wen Liu3,4, Chun-Hui Lang3,4, Xiao-He Luo3,4, Shao-Bo Wu3,4, Xiao-Ping Cui3,4, Zheng Zhou3,4, Man-Man Zhu5, Jing Wang6, Cheng-Jun Xue6, Xiao-Feng Li6, Li Wang6, Zhi-Jie Li7, Kun Wang7, Chang-Chun Niu7, Qing-Jun Yang7, Xiao-Jun Tang8, Yong Zhang ORCID Xia-Mao Liu9, Jin-Jing Li9, De-Chun Zhang10, Fan Zhang10, Ping Liu11, Jun Yuan1, Qin Li12, Jie-Li Hu ORCID Juan Chen ORCID & …Ai-Long Huang ORCID Nature Medicine volume 26, pages 845–848 2020Cite this article 824k Accesses 5536 Citations 4038 Altmetric Metrics details Subjects AbstractWe report acute antibody responses to SARS-CoV-2 in 285 patients with COVID-19. Within 19 days after symptom onset, 100% of patients tested positive for antiviral immunoglobulin-G IgG. Seroconversion for IgG and IgM occurred simultaneously or sequentially. Both IgG and IgM titers plateaued within 6 days after seroconversion. Serological testing may be helpful for the diagnosis of suspected patients with negative RT–PCR results and for the identification of asymptomatic infections. MainThe continued spread of coronavirus disease 2019 COVID-19 has prompted widespread concern around the world, and the World Health Organization WHO, on 11 March 2020, declared COVID-19 a pandemic. Studies on severe acute respiratory syndrome SARS and Middle East respiratory syndrome MERS showed that virus-specific antibodies were detectable in 80–100% of patients at 2 weeks after symptom onset1,2,3,4,5,6. Currently, the antibody responses against SARS-CoV-2 remain poorly understood and the clinical utility of serological testing is total of 285 patients with COVID-19 were enrolled in this study from three designated hospitals; of these patients, 70 had sequential samples available. The characteristics of these patients are summarized in Supplementary Tables 1 and 2. We validated and used a magnetic chemiluminescence enzyme immunoassay MCLIA for virus-specific antibody detection Extended Data Fig. 1a–d and Supplementary Table 3. Serum samples from patients with COVID-19 showed no cross-binding to the S1 subunit of the SARS-CoV spike antigen. However, we did observe some cross-reactivity of serum samples from patients with COVID-19 to nucleocapsid antigens of SARS-CoV Extended Data Fig. 1e. The proportion of patients with positive virus-specific IgG reached 100% approximately 17–19 days after symptom onset, while the proportion of patients with positive virus-specific IgM reached a peak of approximately 20–22 days after symptom onset Fig. 1a and Methods. During the first 3 weeks after symptom onset, there were increases in virus-specific IgG and IgM antibody titers Fig. 1b. However, IgM showed a slight decrease in the >3-week group compared to the ≤3-week group Fig. 1b. IgG and IgM titers in the severe group were higher than those in the non-severe group, although a significant difference was only observed in IgG titer in the 2-week post-symptom onset group Fig. 1c, P = 1 Antibody responses against Graph of positive rates of virus-specific IgG and IgM versus days after symptom onset in 363 serum samples from 262 patients. b, Levels of antibodies against SARS-CoV-2 in patients at different times after symptom onset. c, Comparison of the level of antibodies against SARS-CoV-2 between severe and non-severe patients. The boxplots in b and c show medians middle line and third and first quartiles boxes, while the whiskers show the interquartile range IQR above and below the box. Numbers of patients N are shown underneath. P values were determined with unpaired, two-sided Mann–Whitney DataFull size imageSixty-three patients with confirmed COVID-19 were followed up until discharge. Serum samples were collected at 3-day intervals. Among these, the overall seroconversion rate was 61/63 over the follow-up period. Two patients, a mother and daughter, maintained IgG- and IgM-negative status during hospitalization. Serological courses could be followed for 26 patients who were initially seronegative and then underwent seroconversion during the observation period. All these patients achieved seroconversion of IgG or IgM within 20 days after symptom onset. The median day of seroconversion for both IgG and IgM was 13 days post symptom onset. Three types of seroconversion were observed synchronous seroconversion of IgG and IgM nine patients, IgM seroconversion earlier than that of IgG seven patients and IgM seroconversion later than that of IgG ten patients Fig. 2a. Longitudinal antibody changes in six representative patients of the three types of seroconversion are shown in Fig. 2b–d and Extended Data Fig. 2a– 2 Seroconversion time of the antibodies against Seroconversion type of 26 patients who were initially seronegative during the observation period. The days of seroconversion for each patient are plotted. b–d, Six representative examples of the three seroconversion type synchronous seroconversion of IgG and IgM b, IgM seroconversion earlier than that of IgG c and IgM seroconversion later than that of IgG c.Full size imageIgG levels in the 19 patients who underwent IgG seroconversion during hospitalization plateaued 6 days after the first positive IgG measurement Extended Data Fig. 3. Plateau IgG levels varied widely more than 20-fold across patients. IgM also showed a similar profile of dynamic changes Extended Data Fig. 4. We found no association between plateau IgG levels and the clinical characteristics of the patients Extended Data Fig. 5a–d. We next analyzed whether the criteria for confirmation of MERS-CoV infection recommended by WHO, including 1 seroconversion or 2 a fourfold increase in IgG-specific antibody titers, are suitable for the diagnosis of COVID-19 using paired samples from 41 patients. The initial sample was collected in the first week of illness and the second was collected 2–3 weeks later. Of the patients whose IgG was initially seronegative in the first week of illness, 21/41 underwent seroconversion. A total of 18 patients were initially seropositive in the first week of illness; of these, eight patients had a fourfold increase in virus-specific IgG titers Extended Data Fig. 6. Overall, 29/41 of the patients with COVID-19 met the criteria of IgG seroconversion and/or fourfold increase or greater in the IgG investigate whether serology testing could help identify patients with COVID-19, we screened 52 suspected cases in patients who displayed symptoms of COVID-19 or abnormal radiological findings and for whom testing for viral RNA was negative in at least two sequential samples. Of the 52 suspected cases, four had virus-specific IgG or IgM in the initial samples Extended Data Fig. 7. Patient 3 had a greater than fourfold increase in IgG titer 3 days after the initial serology testing. Interestingly, patient 3 also tested positive for viral infection by polymerase chain reaction with reverse transcription RT–PCR between the two antibody measurements. IgM titer increased over three sequential samples from patient 1 1 was defined as positive and S/CO ≤ 1 as of IgG and IgM against SARS-CoV-2To measure the level of IgG and IgM against SARS-CoV-2, serum samples were collected from the patients. All serum samples were inactivated at 56 °C for 30 min and stored at −20 °C before testing. IgG and IgM against SARS-CoV-2 in plasma samples were tested using MCLIA kits supplied by Bioscience Co. approved by the China National Medical Products Administration; approval numbers 20203400183IgG and 20203400182IgM, according to the manufacturer’s instructions. MCLIA for IgG or IgM detection was developed based on a double-antibody sandwich immunoassay. The recombinant antigens containing the nucleoprotein and a peptide from the spike protein of SARS-CoV-2 were conjugated with FITC and immobilized on anti-FITC antibody-conjugated magnetic particles. Alkaline phosphatase conjugated anti-human IgG/IgM antibody was used as the detection antibody. The tests were conducted on an automated magnetic chemiluminescence analyzer Axceed 260, Bioscience according to the manufacturer’s instructions. All tests were performed under strict biosafety conditions. The antibody titer was tested once per serum sample. Antibody levels are presented as the measured chemiluminescence values divided by the cutoff S/CO. The cutoff value of this test was defined by receiver operating characteristic curves. Antibody levels in the figures were calculated as log2S/CO + 1.Performance evaluation of the SARS-CoV-2-specific IgG/IgM detection assayThe precision and reproducibility of the MCLIA kits were first evaluated by the National Institutes for Food and Drug Control. Moreover, 30 serum samples from patients with COVID-19 showing different titers of IgG range and IgM range were tested. Each individual sample was tested in three independent experiments, and the coefficient of variation CV was used to evaluate the precision of the assay. Finally, 46 serum samples from patients with COVID-19 were assessed using different batches of the diagnostic kit for SARS-CoV-2-specific IgG or IgM antibody; reproducibility was calculated based on the results from two batch of antigens from SARS-CoV and SARS-CoV-2Two recombinant SARS-CoV nucleocapsid N proteins from two different sources Sino Biological, cat. no. 40143-V08B; Biorbyt, cat. no. orb82478, the recombinant S1 subunit of the SARS-CoV spike Sino Biological, cat. no. 40150-V08B1 and the homemade recombinant N protein of SARS-CoV-2 were used in a chemiluminescence enzyme immunoassay CLEIA, respectively. The concentration of antigens used for plate coating was μg ml−1. The dilution of alkaline phosphatase conjugated goat anti-human IgG antibody was 12,500. Five serum samples from patients with COVID-19 and five serum samples from healthy controls were diluted 150 and tested using CLEIA assays. The binding ability of antibody to antigen in a sample was measured in relative luminescence analysesContinuous variables are expressed as the median IQR and were compared with the Mann–Whitney U-test. Categorical variables are expressed as numbers % and were compared by Fisher’s exact test. A P value of < was considered statistically significant. Statistical analyses were performed using R software, version approvalThe study was approved by the Ethics Commission of Chongqing Medical University ref. no. 2020003. Written informed consent was waived by the Ethics Commission of the designated hospital for emerging infectious SummaryFurther information on research design is available in the Nature Research Reporting Summary linked to this article. Data availabilityRaw data in this study are provided in the Supplementary Dataset. Additional supporting data are available from the corresponding authors on request. All requests for raw and analyzed data and materials will be reviewed by the corresponding authors to verify whether the request is subject to any intellectual property or confidentiality obligations. Source data for Fig. 1 and Extended Data Figs. 1 and 5 are available V. M. et al. Viral shedding and antibody response in 37 patients with Middle East respiratory syndrome coronavirus infection. Clin. Infect. Dis. 62, 477–483 2016.CAS PubMed Google Scholar Li, G., Chen, X. & Xu, A. Profile of specific antibodies to the SARS-associated coronavirus. N. Engl. J. Med. 349, 508–509 2003.Article Google Scholar Hsueh, P. R., Huang, L. M., Chen, P. J., Kao, C. L. & Yang, P. C. Chronological evolution of IgM, IgA, IgG and neutralisation antibodies after infection with SARS-associated coronavirus. Clin. Microbiol. Infect. 10, 1062–1066 2004.Article Google Scholar Park, W. B. et al. Kinetics of serologic responses to MERS coronavirus infection in humans, South Korea. Emerg. Infect. Dis. 21, 2186–2189 2015.Article CAS Google Scholar Drosten, C. et al. Transmission of MERS-coronavirus in household contacts. N. Engl. J. Med. 371, 828–835 2014.Article Google Scholar Meyer, B., Drosten, C. & Muller, M. A. Serological assays for emerging coronaviruses challenges and pitfalls. Virus Res. 194, 175–183 2014.Article CAS Google Scholar Tang, Y. W., Schmitz, J. E., Persing, D. H. & Stratton, C. W. The laboratory diagnosis of COVID-19 infection current issues and challenges. J. Clin. Microbiol. 2020.Zou, L. et al. SARS-CoV-2 viral load in upper respiratory specimens of infected patients. N. Engl. J. Med. 382, 1177–1179 2020.Article Google Scholar Download referencesAcknowledgementsWe thank Yang and Kwan for critical reviewing of the manuscript. This work was supported by the Emergency Project from the Science & Technology Commission of Chongqing and a Major National S&T Program grant 2017ZX10202203 and 2017ZX10302201 from the Science & Technology Commission of informationAuthor notesThese authors contributed equally Quan-Xin Long, Bai-Zhong Liu, Hai-Jun Deng, Gui-Cheng Wu, Kun Deng, Yao-Kai and AffiliationsKey Laboratory of Molecular Biology on Infectious Diseases, Ministry of Education, Chongqing Medical University, Chongqing, ChinaQuan-Xin Long, Hai-Jun Deng, Yong Lin, Xue-Fei Cai, De-Qiang Wang, Yuan Hu, Ji-Hua Ren, Ni Tang, Jun Yuan, Jie-Li Hu, Juan Chen & Ai-Long HuangYongchuan Hospital Affiliated to Chongqing Medical University, Chongqing, ChinaBai-Zhong Liu, Yin-Yin Xu, Li-Hua Yu, Zhan Mo, Fang Gong, Xiao-Li Zhang, Wen-Guang Tian & Li HuChongqing University Three Gorges Hospital, Chongqing, ChinaGui-Cheng Wu, Xian-Xiang Zhang, Jiang-Lin Xiang, Hong-Xin Du, Hua-Wen Liu, Chun-Hui Lang, Xiao-He Luo, Shao-Bo Wu, Xiao-Ping Cui & Zheng ZhouChongqing Three Gorges Central Hospital, Chongqing, ChinaGui-Cheng Wu, Xian-Xiang Zhang, Jiang-Lin Xiang, Hong-Xin Du, Hua-Wen Liu, Chun-Hui Lang, Xiao-He Luo, Shao-Bo Wu, Xiao-Ping Cui & Zheng ZhouThe Third Hospital Affiliated to Chongqing Medical University, Chongqing, ChinaKun Deng & Man-Man ZhuDivision of Infectious Diseases, Chongqing Public Health Medical Center, Chongqing, ChinaYao-Kai Chen, Jing Wang, Cheng-Jun Xue, Xiao-Feng Li & Li WangLaboratory Department, Chongqing People’s Hospital, Chongqing, ChinaPu Liao, Zhi-Jie Li, Kun Wang, Chang-Chun Niu & Qing-Jun YangSchool of Public Health and Management, Chongqing Medical University, Chongqing, ChinaJing-Fu Qiu, Xiao-Jun Tang & Yong ZhangThe Second Affiliated Hospital of Chongqing Medical University, Chongqing, ChinaXia-Mao Liu & Jin-Jing LiWanzhou People’s Hospital, Chongqing, ChinaDe-Chun Zhang & Fan ZhangBioScience Co. Ltd, Chongqing, ChinaPing LiuChongqing Center for Disease Control and Prevention, Chongqing, ChinaQin LiAuthorsQuan-Xin LongYou can also search for this author in PubMed Google ScholarBai-Zhong LiuYou can also search for this author in PubMed Google ScholarHai-Jun DengYou can also search for this author in PubMed Google ScholarGui-Cheng WuYou can also search for this author in PubMed Google ScholarKun DengYou can also search for this author in PubMed Google ScholarYao-Kai ChenYou can also search for this author in PubMed Google ScholarPu LiaoYou can also search for this author in PubMed Google ScholarJing-Fu QiuYou can also search for this author in PubMed Google ScholarYong LinYou can also search for this author in PubMed Google ScholarXue-Fei CaiYou can also search for this author in PubMed Google ScholarDe-Qiang WangYou can also search for this author in PubMed Google ScholarYuan HuYou can also search for this author in PubMed Google ScholarJi-Hua RenYou can also search for this author in PubMed Google ScholarNi TangYou can also search for this author in PubMed Google ScholarYin-Yin XuYou can also search for this author in PubMed Google ScholarLi-Hua YuYou can also search for this author in PubMed Google ScholarZhan MoYou can also search for this author in PubMed Google ScholarFang GongYou can also search for this author in PubMed Google ScholarXiao-Li ZhangYou can also search for this author in PubMed Google ScholarWen-Guang TianYou can also search for this author in PubMed Google ScholarLi HuYou can also search for this author in PubMed Google ScholarXian-Xiang ZhangYou can also search for this author in PubMed Google ScholarJiang-Lin XiangYou can also search for this author in PubMed Google ScholarHong-Xin DuYou can also search for this author in PubMed Google ScholarHua-Wen LiuYou can also search for this author in PubMed Google ScholarChun-Hui LangYou can also search for this author in PubMed Google ScholarXiao-He LuoYou can also search for this author in PubMed Google ScholarShao-Bo WuYou can also search for this author in PubMed Google ScholarXiao-Ping CuiYou can also search for this author in PubMed Google ScholarZheng ZhouYou can also search for this author in PubMed Google ScholarMan-Man ZhuYou can also search for this author in PubMed Google ScholarJing WangYou can also search for this author in PubMed Google ScholarCheng-Jun XueYou can also search for this author in PubMed Google ScholarXiao-Feng LiYou can also search for this author in PubMed Google ScholarLi WangYou can also search for this author in PubMed Google ScholarZhi-Jie LiYou can also search for this author in PubMed Google ScholarKun WangYou can also search for this author in PubMed Google ScholarChang-Chun NiuYou can also search for this author in PubMed Google ScholarQing-Jun YangYou can also search for this author in PubMed Google ScholarXiao-Jun TangYou can also search for this author in PubMed Google ScholarYong ZhangYou can also search for this author in PubMed Google ScholarXia-Mao LiuYou can also search for this author in PubMed Google ScholarJin-Jing LiYou can also search for this author in PubMed Google ScholarDe-Chun ZhangYou can also search for this author in PubMed Google ScholarFan ZhangYou can also search for this author in PubMed Google ScholarPing LiuYou can also search for this author in PubMed Google ScholarJun YuanYou can also search for this author in PubMed Google ScholarQin LiYou can also search for this author in PubMed Google ScholarJie-Li HuYou can also search for this author in PubMed Google ScholarJuan ChenYou can also search for this author in PubMed Google ScholarAi-Long HuangYou can also search for this author in PubMed Google ScholarContributionsConceptualization was provided by The methodology was developed by P. Liu, and Investigations were carried out by and The original draft of the manuscript was written by and Review and editing of the manuscript were carried out by and Funding acquisition was performed by and Resources were provided by P. Liao, . and provided authorsCorrespondence to Jie-Li Hu, Juan Chen or Ai-Long declarations Competing interests The authors declare no competing interests. Additional informationPeer review information Saheli Sadanand was the primary editor on this article and managed its editorial process and peer review in collaboration with the rest of the editorial note Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional dataExtended Data Fig. 1 The performance evaluation of the SARS-CoV-2 specific IgG/IgM detection Thirty serum sample from COVID-19 patients showing different titers of IgG a range from to and IgM b range from to were tested. Each individual sample was tested in three independent experiment. CVs of titers of certain sample were calculated and presented. c,d. The correlation analysis of IgG and IgM titers serum samples from COVID-19 patients from 2 independent experiment. Forty-six serum samples from COVID-19 patients were detected using different batches of diagnostic kit for SARS-CoV-2 IgG c or IgM d antibody. Pearson correlation coefficients R are depicted in plots. For IgG, r = p = For IgM, r = p = e. The reactivity between COVID-19 patient serums N = 5 and SARS-CoV S1, N two sources and SARS-CoV-2 N protein were measured by ELISA. Serum samples from COVID-19 patients showed no cross-binding to SARS-CoV S1 antigen, while the reactivity between COVID-19 patient serums and SARS-CoV N antigen from different sources was inconsistent. Source Data Extended Data Fig. 2 Three types of Patients with a synchronous seroconversion of IgG and IgM N = 7. b. Seroconversion for IgG occurred later than that for IgMN = 5. c. Seroconversion for IgG occurred earlier than that for IgM N = 8.Extended Data Fig. 3 Dynamic changes of the SARS-CoV-2 specific course of the virus-specific IgG level in 19 patients experienced IgG titer plateau. IgG in each patient reached plateau within 6 days since IgG became Data Fig. 4 Dynamic changes of the SARS-CoV-2 specific course of the virus-specific IgM level in 20 patients experienced IgM titer plateau. IgM in each patient reached plateau within 6 days since IgM became Data Fig. 5 The association between the IgG levels at the plateau and clinical characteristics of the COVID-19 No significant difference in the IgG levels at the plateau was found between < 60 y group N = 11 and ≥ 60 y group N = 9. Unpaired, two-sided Mann-Whitney U test, p = b–d. No association was found between the IgG levels at the plateau and lymphocyte count b or CRP c or hospital stay d of the patients N = 20. Pearson correlation coefficients r and p value are depicted in plots. Source Data Extended Data Fig. 6 The assessment of MERS serological criteria for assessment of MERS serological criteria for COVID-19 confirmation were carried out in 41 patients with sequential samples. All 41 patients were classified into three groups based on IgG change from sequential samples, including 1 seroconversion, 2 fold change ≥ 4-fold in paired samples, 3 Data Fig. 7 Serology testing in identification of COVID-19 from 52 suspected of symptom onset, RT-PCR and serology testing in 4 cases developing positive IgG or/and IgM were Data Fig. 8 Serological survey in close contacts with COVID-19 cluster of 164 close contacts of known COVID-19 patients were tested by RT-PCR followed by serology testing. Serum samples were collected from these 164 individuals for antibody tests approximately 30 days after informationSource dataRights and permissionsAbout this articleCite this articleLong, QX., Liu, BZ., Deng, HJ. et al. Antibody responses to SARS-CoV-2 in patients with COVID-19. Nat Med 26, 845–848 2020. citationReceived 24 March 2020Accepted 22 April 2020Published 29 April 2020Issue Date June 2020DOI This article is cited by

^{JualSd Bio Ag Standard Q Harga Murah, One Step Test is a rapid chromatographic immunoassay for the qualitative detection of specific antigens to SARS-CoV-2 present in human nasopharynx. Fast results within 15~30 mins. Easy to use. 09COV30D.} . 2022 Jan;941388-392. doi Epub 2021 Aug 31. Affiliations PMID 34415572 PMCID PMC8426838 DOI Free PMC article Correlation between a quantitative anti-SARS-CoV-2 IgG ELISA and neutralization activity Ramona Dolscheid-Pommerich et al. J Med Virol. 2022 Jan. Free PMC article Abstract In the current COVID-19 pandemic, a better understanding of the relationship between merely binding and functionally neutralizing antibodies is necessary to characterize protective antiviral immunity following infection or vaccination. This study analyzes the level of correlation between the novel quantitative EUROIMMUN Anti-SARS-CoV-2 QuantiVac ELISA IgG and a microneutralization assay. A panel of 123 plasma samples from a COVID-19 outbreak study population, preselected by semiquantitative anti-SARS-CoV-2 IgG testing, was used to assess the relationship between the novel quantitative ELISA IgG and a microneutralization assay. Binding IgG targeting the S1 antigen was detected in 106 samples using the QuantiVac ELISA, while 89 samples showed neutralizing antibody activity. Spearman's correlation analysis demonstrated a strong positive relationship between anti-S1 IgG levels and neutralizing antibody titers rs = p < High and low anti-S1 IgG levels were associated with a positive predictive value of for high-titer neutralizing antibodies and a negative predictive value of for low-titer neutralizing antibodies, respectively. These results substantiate the implementation of the QuantiVac ELISA to assess protective immunity following infection or vaccination. Keywords COVID-19; ELISA; SARS-CoV-2; microneutralization. © 2021 The Authors. Journal of Medical Virology Published by Wiley Periodicals LLC. Conflict of interest statement Sandra Saschenbrecker and Katja Steinhagen are employed by EUROIMMUN Medizinische Labordiagnostika AG, a manufacturer of diagnostic reagents and co‐owner of a patent application pertaining to the detection of antibodies to the SARS‐CoV‐2 S1 antigen. Katja Steinhagen is designated as an inventor. The other authors declare that there are no conflict of interests. Figures Figure 1 Correlation between quantitative ELISA and microneutralization assay. Binding anti‐SARS‐CoV‐2 S1 IgG was determined quantitatively using the QuantiVac ELISA and titers of neutralizing antibodies were determined using the CPE reduction NT assay n = 123. Neutralization titers correspond to reciprocal plasma dilutions protecting 50% of the wells at incubation with 100 TCID50 of SARS‐CoV‐2. Samples with a cytopathic effect CPE equal or similar to the negative control are depicted on the y‐axis. Dotted and dashed lines indicate borderline and positivity cut‐offs, respectively. r s, Spearman rank‐order correlation coefficient Similar articles Inference of SARS-CoV-2 spike-binding neutralizing antibody titers in sera from hospitalized COVID-19 patients by using commercial enzyme and chemiluminescent immunoassays. Valdivia A, Torres I, Latorre V, Francés-Gómez C, Albert E, Gozalbo-Rovira R, Alcaraz MJ, Buesa J, Rodríguez-Díaz J, Geller R, Navarro D. Valdivia A, et al. Eur J Clin Microbiol Infect Dis. 2021 Mar;403485-494. doi Epub 2021 Jan 6. Eur J Clin Microbiol Infect Dis. 2021. PMID 33404891 Free PMC article. SARS-CoV-2 Serologic Assays in Control and Unknown Populations Demonstrate the Necessity of Virus Neutralization Testing. Rathe JA, Hemann EA, Eggenberger J, Li Z, Knoll ML, Stokes C, Hsiang TY, Netland J, Takehara KK, Pepper M, Gale M Jr. Rathe JA, et al. J Infect Dis. 2021 Apr 8;22371120-1131. doi J Infect Dis. 2021. PMID 33367830 Free PMC article. A highly specific and sensitive serological assay detects SARS-CoV-2 antibody levels in COVID-19 patients that correlate with neutralization. Peterhoff D, Glück V, Vogel M, Schuster P, Schütz A, Neubert P, Albert V, Frisch S, Kiessling M, Pervan P, Werner M, Ritter N, Babl L, Deichner M, Hanses F, Lubnow M, Müller T, Lunz D, Hitzenbichler F, Audebert F, Hähnel V, Offner R, Müller M, Schmid S, Burkhardt R, Glück T, Koller M, Niller HH, Graf B, Salzberger B, Wenzel JJ, Jantsch J, Gessner A, Schmidt B, Wagner R. Peterhoff D, et al. Infection. 2021 Feb;49175-82. doi Epub 2020 Aug 21. Infection. 2021. PMID 32827125 Free PMC article. Quantitative SARS-CoV-2 Serology in Children With Multisystem Inflammatory Syndrome MIS-C. Rostad CA, Chahroudi A, Mantus G, Lapp SA, Teherani M, Macoy L, Tarquinio KM, Basu RK, Kao C, Linam WM, Zimmerman MG, Shi PY, Menachery VD, Oster ME, Edupuganti S, Anderson EJ, Suthar MS, Wrammert J, Jaggi P. Rostad CA, et al. Pediatrics. 2020 Dec;1466e2020018242. doi Epub 2020 Sep 2. Pediatrics. 2020. PMID 32879033 Recent Developments in SARS-CoV-2 Neutralizing Antibody Detection Methods. Banga Ndzouboukou JL, Zhang YD, Fan XL. Banga Ndzouboukou JL, et al. Curr Med Sci. 2021 Dec;4161052-1064. doi Epub 2021 Dec 21. Curr Med Sci. 2021. PMID 34935114 Free PMC article. Review. Cited by Impact of Health Workers' Choice of COVID-19 Vaccine Booster on Immunization Levels in Istanbul, Turkey. Ören MM, Canbaz S, Meşe S, Ağaçfidan A, Demir ÖS, Karaca E, Doğruyol AR, Otçu GH, Tükek T, Özgülnar N. Ören MM, et al. Vaccines Basel. 2023 May 3;115935. doi Vaccines Basel. 2023. PMID 37243039 Free PMC article. Development and validity assessment of ELISA test with recombinant chimeric protein of SARS-CoV-2. Fernandez Z, de Arruda Rodrigues R, Torres JM, Marcon GEB, de Castro Ferreira E, de Souza VF, Sarti EFB, Bertolli GF, Araujo D, Demarchi LHF, Lichs G, Zardin MU, Gonçalves CCM, Cuenca V, Favacho A, Guilhermino J, Dos Santos LR, de Araujo FR, Silva MR. Fernandez Z, et al. J Immunol Methods. 2023 May 11;519113489. doi Online ahead of print. J Immunol Methods. 2023. PMID 37179011 Free PMC article. Dynamics of Antibody Responses after Asymptomatic and Mild to Moderate SARS-CoV-2 Infections Real-World Data in a Resource-Limited Country. Sayabovorn N, Phisalprapa P, Srivanichakorn W, Chaisathaphol T, Washirasaksiri C, Sitasuwan T, Tinmanee R, Kositamongkol C, Nimitpunya P, Mepramoon E, Ariyakunaphan P, Woradetsittichai D, Chayakulkeeree M, Phoompoung P, Mayurasakorn K, Sookrung N, Tungtrongchitr A, Wanitphakdeedecha R, Muangman S, Senawong S, Tangjittipokin W, Sanpawitayakul G, Nopmaneejumruslers C, Vamvanij V, Auesomwang C. Sayabovorn N, et al. Trop Med Infect Dis. 2023 Mar 23;84185. doi Trop Med Infect Dis. 2023. PMID 37104311 Free PMC article. Convalescent Plasma Treatment of Patients Previously Treated with B-Cell-Depleting Monoclonal Antibodies Suffering COVID-19 Is Associated with Reduced Re-Admission Rates. Ioannou P, Katsigiannis A, Papakitsou I, Kopidakis I, Makraki E, Milonas D, Filippatos TD, Sourvinos G, Papadogiannaki M, Lydaki E, Chamilos G, Kofteridis DP. Ioannou P, et al. Viruses. 2023 Mar 15;153756. doi Viruses. 2023. PMID 36992465 Free PMC article. Characterisation of the Antibody Response in Sinopharm BBIBP-CorV Recipients and COVID-19 Convalescent Sera from the Republic of Moldova. Ulinici M, Suljič A, Poggianella M, Milan Bonotto R, Resman Rus K, Paraschiv A, Bonetti AM, Todiras M, Corlateanu A, Groppa S, Ceban E, Petrovec M, Marcello A. Ulinici M, et al. Vaccines Basel. 2023 Mar 13;113637. doi Vaccines Basel. 2023. PMID 36992221 Free PMC article. References Krammer F, Simon F. Serology assays to manage COVID‐19. Science. 2020;3681060‐1061. - PubMed Lee CY, Lin RTP, Renia L, Ng LFP. Serological approaches for COVID‐19 Epidemiologic perspective on surveillance and control. Front Immunol. 2020;11879. - PMC - PubMed Theel ES, Slev P, Wheeler S, Couturier MR, Wong SJ, Kadkhoda K. The role of antibody testing for SARS‐CoV‐2 is there one? J Clin Microbiol. 2020;5858. - PMC - PubMed Zost SJ, Gilchuk P, Case JB, et al. Potently neutralizing and protective human antibodies against SARS‐CoV‐2. Nature. 2020;584443‐449. - PMC - PubMed Rogers TF, Zhao F, Huang D, et al. Isolation of potent SARS‐CoV‐2 neutralizing antibodies and protection from disease in a small animal model. Science. 2020;369956‐963. - PMC - PubMed Publication types MeSH terms Substances LinkOut - more resources Full Text Sources Europe PubMed Central Ovid Technologies, Inc. PubMed Central Wiley Medical Genetic Alliance Miscellaneous NCI CPTAC Assay Portal

PemeriksaanAnti SARS-CoV-2 Kuantitatif disarankan bagi penyintas COVID-19 atau orang yang pernah terinfeksi COVID-19, pasien pasca vaksinasi COVID-19, dan terapi plasma konvalesen (skrining pendonor dan pemantauan resipien). Pemeriksaan Anti SARS-CoV-2 Kuantitatif dilakukan umumnya 14 hari setelah dosis vaksin terakhir diberikan sudah terjadi

. 2021 Dec;93126813-6817. doi Epub 2021 Aug 5. Affiliations PMID 34314037 PMCID PMC8427121 DOI Free PMC article The dynamics of quantitative SARS-CoV-2 antispike IgG response to BNT162b2 vaccination Shun Kaneko et al. J Med Virol. 2021 Dec. Free PMC article Abstract Vaccination for SARS-CoV-2 is necessary to overcome coronavirus disease 2019 COVID-19. However, the time-dependent vaccine-induced immune response is not well understood. This study aimed to investigate the dynamics of SARS-CoV-2 antispike immunoglobulin G IgG response. Medical staff participants who received two sequential doses of the BNT162b2 vaccination on days 0 and 21 were recruited prospectively from the Musashino Red Cross Hospital between March and May 2021. The quantitative antispike receptor-binding domain RBD IgG antibody responses were measured using the Abbott SARS-CoV-2 IgGII Quant assay cut off ≥50 AU/ml. A total of 59 participants without past COVID-19 history were continuously tracked with serum samples. The median age was 41 22-75 years, and 14 participants were male The median antispike RBD IgG and seropositivity rates were 0 AU/ml, AU/ml, AU/ml, 18, AU/ml, and 0%, 0%, and 100% on days 0, 3, 14, and 28 after the first vaccination, respectively. The antispike RBD IgG levels were significantly increased after day 14 from vaccination p < The BNT162b2 vaccination led almost all participants to obtain serum antispike RBD IgG 14 days after the first dose. Keywords COVID-19; SARS-Cov-2; mRNA vaccine; quantitative antispike RBD IgG. © 2021 Wiley Periodicals LLC. Conflict of interest statement The authors declare that there are no conflict of interests. Figures Figure 1 Dynamics of SARS‐CoV‐2 antispike RBD IgG response after vaccination. A Schema of the schedule for vaccination and blood test. B Antispike RBD IgG titer AU/ml and seropositive rate of antispike RBD IgG and antinucleocapsid IgG in a time‐dependent manner. RBD, receptor‐binding domain Similar articles Evaluation of Humoral Immune Response after SARS-CoV-2 Vaccination Using Two Binding Antibody Assays and a Neutralizing Antibody Assay. Nam M, Seo JD, Moon HW, Kim H, Hur M, Yun YM. Nam M, et al. Microbiol Spectr. 2021 Dec 22;93e0120221. doi Epub 2021 Nov 24. Microbiol Spectr. 2021. PMID 34817223 Free PMC article. Healthcare Workers in South Korea Maintain a SARS-CoV-2 Antibody Response Six Months After Receiving a Second Dose of the BNT162b2 mRNA Vaccine. Choi JH, Kim YR, Heo ST, Oh H, Kim M, Lee HR, Yoo JR. Choi JH, et al. Front Immunol. 2022 Jan 31;13827306. doi eCollection 2022. Front Immunol. 2022. PMID 35173736 Free PMC article. Evaluation of Seropositivity Following BNT162b2 Messenger RNA Vaccination for SARS-CoV-2 in Patients Undergoing Treatment for Cancer. Massarweh A, Eliakim-Raz N, Stemmer A, Levy-Barda A, Yust-Katz S, Zer A, Benouaich-Amiel A, Ben-Zvi H, Moskovits N, Brenner B, Bishara J, Yahav D, Tadmor B, Zaks T, Stemmer SM. Massarweh A, et al. JAMA Oncol. 2021 Aug 1;781133-1140. doi JAMA Oncol. 2021. PMID 34047765 Free PMC article. Evaluation of the SARS-CoV-2 Antibody Response to the BNT162b2 Vaccine in Patients Undergoing Hemodialysis. Yau K, Abe KT, Naimark D, Oliver MJ, Perl J, Leis JA, Bolotin S, Tran V, Mullin SI, Shadowitz E, Gonzalez A, Sukovic T, Garnham-Takaoka J, de Launay KQ, Takaoka A, Straus SE, McGeer AJ, Chan CT, Colwill K, Gingras AC, Hladunewich MA. Yau K, et al. JAMA Netw Open. 2021 Sep 1;49e2123622. doi JAMA Netw Open. 2021. PMID 34473256 Free PMC article. Review of SARS-CoV-2 Antigen and Antibody Testing in Diagnosis and Community Surveillance. Nerenz RD, Hubbard JA, Cervinski MA. Nerenz RD, et al. Clin Lab Med. 2022 Dec;424687-704. doi Clin Lab Med. 2022. PMID 36368790 Free PMC article. Review. No abstract available. Cited by Higher Immunological Response after BNT162b2 Vaccination among COVID-19 Convalescents-The Data from the Study among Healthcare Workers in an Infectious Diseases Center. Skrzat-Klapaczyńska A, Kowalska JD, Paciorek M, Puła J, Bieńkowski C, Krogulec D, Stengiel J, Pawełczyk A, Perlejewski K, Osuch S, Radkowski M, Horban A. Skrzat-Klapaczyńska A, et al. Vaccines Basel. 2022 Dec 15;10122158. doi Vaccines Basel. 2022. PMID 36560567 Free PMC article. Measurements of Anti-SARS-CoV-2 Antibody Levels after Vaccination Using a SH-SAW Biosensor. Cheng CH, Peng YC, Lin SM, Yatsuda H, Liu SH, Liu SJ, Kuo CY, Wang RYL. Cheng CH, et al. Biosensors Basel. 2022 Aug 4;128599. doi Biosensors Basel. 2022. PMID 36004995 Free PMC article. Relationship between changes in symptoms and antibody titers after a single vaccination in patients with Long COVID. Tsuchida T, Hirose M, Inoue Y, Kunishima H, Otsubo T, Matsuda T. Tsuchida T, et al. J Med Virol. 2022 Jul;9473416-3420. doi Epub 2022 Mar 8. J Med Virol. 2022. PMID 35238053 Free PMC article. The Comparability of Anti-Spike SARS-CoV-2 Antibody Tests is Time-Dependent a Prospective Observational Study. Perkmann T, Mucher P, Perkmann-Nagele N, Radakovics A, Repl M, Koller T, Schmetterer KG, Bigenzahn JW, Leitner F, Jordakieva G, Wagner OF, Binder CJ, Haslacher H. Perkmann T, et al. Microbiol Spectr. 2022 Feb 23;101e0140221. doi Epub 2022 Feb 23. Microbiol Spectr. 2022. PMID 35196824 Free PMC article. References Guan WJ, Ni ZY, Hu Y, et al. Clinical characteristics of coronavirus disease 2019 in China. N Engl J Med. 2020;382181708‐1720. - PMC - PubMed Zhou F, Yu T, Du R, et al. Clinical course and risk factors for mortality of adult inpatients with COVID‐19 in Wuhan, China a retrospective cohort study. Lancet. 2020;395102291054‐1062. - PMC - PubMed Zheng Z, Peng F, Xu B, et al. Risk factors of critical & mortal COVID‐19 cases a systematic literature review and meta‐analysis. J Infect. 2020;8116. - PMC - PubMed Hu Y, Sun J, Dai Z, et al. Prevalence and severity of corona virus disease 2019 COVID‐19 a systematic review and meta‐analysis. J Clin Virol. 2020;127104371. - PMC - PubMed World Health Organization . Coronavirus disease COVID‐19. Situation report. Accessed, May 17th, MeSH terms Substances LinkOut - more resources Full Text Sources Europe PubMed Central Ovid Technologies, Inc. PubMed Central Wiley Medical Genetic Alliance MedlinePlus Health Information Miscellaneous NCI CPTAC Assay Portal

Titerantibodi yang diperiksa dalam pemeriksaan Anti SARS-CoV-2 Kuantitatif ini adalah antibodi terhadap protein khusus dari virus penyebab Covid-19, yaitu protein spike-RBD (Spike-Receptor Binding Domain). Antibodi tersebut dapat terbentuk tidak hanya oleh vaksinasi, tetapi infeksi alami yang juga memicu tubuh membentuk antibodi. ^{- Seperti diketahui, orang yang sudah pernah terinfeksi Covid-19 akan memiliki kekebalan tubuh atau antibodi terhadap serangan virus SARS-CoV-2 penyebab Covid-19 di masa depan. Namun, seberapa besar kekebalan tubuh orang yang pernah terpapar Covid-19?Mengenai persoalan ini, Dokter Spesialis Patologi Klinik Primaya Hospital Bekasi Barat dan Bekasi Timur, dr Muhammad Irhamsyah SpPK MKes angkat bicara. Irhamsyah menjelaskan bahwa terdapat metode pemeriksaan kekebalan tubuh manusia terhadap Covid-19 melalui pemeriksaan Antibodi SARS-CoV-2 kuantitatif. Baca juga Daftar 5 Kelompok Prioritas Vaksinasi Covid-19 Tahap Kedua, dari Guru hingga Pedagang Pemeriksaan Antibodi SARS-CoV-2 suatu pemeriksaan untuk mendeteksi suatu protein yang disebut antibodi, khususnya antibodi spesifik terhadap SARS-CoV-2 ini."Pemeriksaan ini dapat dilakukan pada orang-orang yang sudah pernah terinfeksi Covid-19, orang yang sudah mendapatkan vaksinasi, serta dapat digunakan untuk mengukur antibodi pada donor plasma konvalesen yang akan ditransfusikan,” kata Irhamsyah. Cara kerja pemeriksaan kuantitatif antibodi ECLIA Dijelaskan dr Irhamsyah, prinsip pemeriksaan kuantitatif antibodi spesifik SARS-CoV-2 ini menggunakan pemeriksaan laboratorium imunoserologi pada sebuah alat automatik autoanalyzer. Alat automatik ini dipergunakan untuk mendeteksi antibodi terhadap SAR-CoV-2. Pemeriksaan ini biasa disebut dengan Electro Chemiluminescence Immunoasssay ECLIA. ECLIA akan mendeteksi, mengikat, serta mengukur antibodi netralisasi. Sebagai informasi, antibodi netralisasi adalah antibodi yang dapat berikatan spesifik pada bagian struktur protein spike SARS-CoV-2. Protein spike adalah protein berbentuk paku yang tersebar di permukaan virus Covid-19, sebelum virus Covid-19 memasuki sel-sel pada tubuh kita dengan menggunakan label-label yang berikatan spesifik dengan antibodi netralisasi tersebut. Adapun, jenis sampel yang dapat digunakan dalam pemeriksaan ini yaitu sampel serum dan plasma dengan cara diambil darah vena.}

Pemeriksaan Anti SARS-CoV-2 Kuantitatif dapat memantau imun tubuh terhadap vaksin dengan satuan . angka U/mL - Pemeriksaan Anti SARS-CoV-2 Kuantitatif dapat melihat tingkat antibody sebagai penentu seseorang dapat . melakukan donor

. 2021 Aug 18;599e0028821. doi Epub 2021 Aug 18. Affiliations PMID 34260272 PMCID PMC8373017 DOI Free PMC article Performance of the Abbott SARS-CoV-2 IgG II Quantitative Antibody Assay Including the New Variants of Concern, VOC 202012/V1 United Kingdom and VOC 202012/V2 South Africa, and First Steps towards Global Harmonization of COVID-19 Antibody Methods Emma English et al. J Clin Microbiol. 2021. Free PMC article Abstract In the initial stages of the severe acute respiratory syndrome coronavirus 2 SARS-CoV-2 COVID-19 pandemic, a plethora of new serology tests were developed and introduced to the global market. Many were not evaluated rigorously, and there is a significant lack of concordance in results across methods. To enable meaningful clinical decisions to be made, robustly evaluated, quantitative serology methods are needed. These should be harmonized to a primary reference material, allowing for the comparison of trial data and improved clinical decision making. A comprehensive evaluation of the new Abbott IgG II anti-SARS-CoV-2 IgG method was undertaken using CLSI-based protocols. Two different candidate primary reference materials and verification panels were assessed with a goal to move toward harmonization. The Abbott IgG II method performed well across a wide range of parameters with excellent imprecision < and was linear throughout the positive range tested to 38,365 AU/ml. The sensitivity based on ≥14-day post-positive reverse transcription-PCR [RT-PCR] samples and specificity were to and to 100%, respectively. The candidate reference materials showed poor correlation across methods, with mixed responses noted in methods that use the spike protein versus the nucleocapsid proteins as their binding antigen. The Abbott IgG II anti-SARS-CoV-2 measurement appears to be the first linear method potentially capable of monitoring the immune response to natural infection, including from new emerging variants. The candidate reference materials assessed did not generate uniform results across several methods, and further steps are needed to enable the harmonization process. Keywords COVID-19; SARS-CoV-2; analytical performance; antibody assay; evaluation; harmonization; serology; variants. Figures FIG 1 Linearity of method over the complete working range of the Abbott IgG II assay using a range of dilutions of a high positive mean, 38,365 AU/ml in the Abbott diluent. Dash-dot line indicates the identity line. The darker dotted line represents the 95% likelihood asymmetrical CI of the slope. FIG 2 Cohen’s kappa concordance analysis of the assays and overall all samples included agreement of results given as percent. Equivocal results were considered negative. FIG 3 Representative examples of the quantitative immune response in three different variants of the SARS-CoV-2 virus, including the “UK” and “South Africa” variants. The days post-PCR do not necessarily correlate to the day of onset of symptoms or the day of hospitalization. FIG 4 Comparison graphs of the values obtained for the Technopath positive panel with different methods A Abbott IgG II versus DiaSorin Liaison XL; B Abbott IgG II versus EDI; C Abbott IgG II quantitative S versus Abbott IgG qualitative R. Only the Abbott quantitative assay showed linearity r2 = and was plotted against DiaSorin, quadratic r2 = A, EDI, 4-PL r2 = B, and Abbott qualitative, 4-PL r2 = C. FIG 5 Dilution of NIBSC working standard 20/162 using the Abbott diluent. Dash-dot line indicates the identity line. The darker dotted line represents the 95% likelihood asymmetrical CI of the slope. Similar articles Clinical and analytical evaluation of the Abbott AdviseDx quantitative SARS-CoV-2 IgG assay and comparison with two other serological tests. Maine GN, Krishnan SM, Walewski K, Trueman J, Sykes E, Sun Q. Maine GN, et al. J Immunol Methods. 2022 Apr;503113243. doi Epub 2022 Feb 16. J Immunol Methods. 2022. PMID 35181288 Free PMC article. SARS-CoV-2 Antibody Testing in Health Care Workers A Comparison of the Clinical Performance of Three Commercially Available Antibody Assays. Allen N, Brady M, Carrion Martin AI, Domegan L, Walsh C, Houlihan E, Kerr C, Doherty L, King J, Doheny M, Griffin D, Molloy M, Dunne J, Crowley V, Holmes P, Keogh E, Naughton S, Kelly M, O'Rourke F, Lynagh Y, Crowley B, de Gascun C, Holder P, Bergin C, Fleming C, Ni Riain U, Conlon N; PRECISE Study Steering Group. Allen N, et al. Microbiol Spectr. 2021 Oct 31;92e0039121. doi Epub 2021 Sep 29. Microbiol Spectr. 2021. PMID 34585976 Free PMC article. A Qualitative Comparison of the Abbott SARS-CoV-2 IgG II Quant Assay against Commonly Used Canadian SARS-CoV-2 Enzyme Immunoassays in Blood Donor Retention Specimens, April 2020 to March 2021. Abe KT, Rathod B, Colwill K, Gingras AC, Tuite A, Robbins NF, Orjuela G, Jenkins C, Conrod V, Yi QL, O'Brien SF, Drews SJ. Abe KT, et al. Microbiol Spectr. 2022 Jun 29;103e0113422. doi Epub 2022 Jun 2. Microbiol Spectr. 2022. PMID 35652636 Free PMC article. Efficacy of frontline chemical biocides and disinfection approaches for inactivating SARS-CoV-2 variants of concern that cause coronavirus disease with the emergence of opportunities for green eco-solutions. Rowan NJ, Meade E, Garvey M. Rowan NJ, et al. Curr Opin Environ Sci Health. 2021 Oct;23100290. doi Epub 2021 Jul 3. Curr Opin Environ Sci Health. 2021. PMID 34250323 Free PMC article. Review. Recapping the Features of SARS-CoV-2 and Its Main Variants Status and Future Paths. Ortega MA, García-Montero C, Fraile-Martinez O, Colet P, Baizhaxynova A, Mukhtarova K, Alvarez-Mon M, Kanatova K, Asúnsolo A, Sarría-Santamera A. Ortega MA, et al. J Pers Med. 2022 Jun 18;126995. doi J Pers Med. 2022. PMID 35743779 Free PMC article. Review. Cited by The changing profile of SARS-CoV-2 serology in Irish blood donors. Coyne D, Butler D, Meehan A, Keogh E, Williams P, Carterson A, Hervig T, O'Flaherty N, Waters A. Coyne D, et al. Glob Epidemiol. 2023 Dec;5100108. doi Epub 2023 Apr 21. Glob Epidemiol. 2023. PMID 37122774 Free PMC article. Mix-and-match COVID-19 vaccines trigger high antibody response after the third dose vaccine in Moroccan health care workers. Amellal H, Assaid N, Akarid K, Maaroufi A, Ezzikouri S, Sarih M. Amellal H, et al. Vaccine X. 2023 Aug;14100288. doi Epub 2023 Mar 25. Vaccine X. 2023. PMID 37008956 Free PMC article. Impact of MERS-CoV and SARS-CoV-2 Viral Infection on Immunoglobulin-IgG Cross-Reactivity. AlKhalifah JM, Seddiq W, Alshehri MA, Alhetheel A, Albarrag A, Meo SA, Al-Tawfiq JA, Barry M. AlKhalifah JM, et al. Vaccines Basel. 2023 Feb 26;113552. doi Vaccines Basel. 2023. PMID 36992136 Free PMC article. Dynamics of Anti-S IgG Antibodies Titers after the Second Dose of COVID-19 Vaccines in the Manual and Craft Worker Population of Qatar. Bansal D, Atia H, Al Badr M, Nour M, Abdulmajeed J, Hasan A, Al-Hajri N, Ahmed L, Ibrahim R, Zamel R, Mohamed A, Pattalaparambil H, Daraan F, Chaudhry A, Oraby S, El-Saleh S, El-Shafie SS, Al-Farsi AF, Paul J, Ismail A, Al-Romaihi HE, Al-Thani MH, Doi SAR, Zughaier SM, Cyprian F, Farag E, Farooqui HH. Bansal D, et al. Vaccines Basel. 2023 Feb 21;113496. doi Vaccines Basel. 2023. PMID 36992080 Free PMC article. Quantification of Severe Acute Respiratory Syndrome Coronavirus 2 Binding Antibody Levels To Assess Infection and Vaccine-Induced Immunity Using WHO Standards. Pernet O, Balog S, Kawaguchi ES, Lam CN, Anthony P, Simon P, Kotha R, Sood N, Hu H, Kovacs A. Pernet O, et al. Microbiol Spectr. 2023 Feb 14;111e0370922. doi Epub 2023 Jan 23. Microbiol Spectr. 2023. PMID 36688648 Free PMC article. References Worldometer. 2021. COVID-19 coronavirus pandemic. Dover, DE, USA. Accessed 10 January 2021. World Health Organization. 2021. Weekly epidemiological update on COVID-19 – 16 March 2021. World Health Organization, Geneva, Switzerland. Krammer F. 2020. SARS-CoV-2 vaccines in development. Nature 586516–527. - DOI - PubMed Department of Health and Social Care. 2021. UK COVID-19 vaccines delivery plan. Department of Health and Social Care, London, United Kingdom. Khoury DS, Wheatley AK, Ramuta MD, Reynaldi A, Cromer D, Subbarao K, O'Connor DH, Kent SJ, Davenport MP. 2020. Measuring immunity to SARS-CoV-2 infection comparing assays and animal models. Nat Rev Immunol 20727–738. - DOI - PMC - PubMed Publication types MeSH terms Substances LinkOut - more resources Full Text Sources Atypon Europe PubMed Central PubMed Central Medical Genetic Alliance MedlinePlus Health Information Miscellaneous NCI CPTAC Assay Portal

SARSCOV-2, S5-S6 positif atau negatif untuk SARS-CoV-2. 2. Tingkat kebetulan positif: PC1-PC8 positif untuk SARS-CoV-2. 3. Tingkat kebetulan negatif: NC1-NC20 negatif untuk SARS-CoV-2. 4. Pengulangan: CV1-CV2 positif untuk SARS-CoV-2. 5. Presisi antar batch: 3 batch perangkat ini dapat digunakan untuk menguji pengulangan, dan hasil yang sesuai

The development timeline of COVID-19 vaccines is unprecedented, with more than 300 vaccine developers active worldwide. Vaccine candidates developed with various technology platforms targeting different epitopes of SARS-CoV-2 are in the pipeline. Vaccine developers are using a range of immunoassays with different readouts to measure immune responses after vaccination, making comparisons of the immunogenicity of different COVID-19 vaccine candidates April, 2020, in a joint effort, the Coalition for Epidemic Preparedness Innovations CEPI, the National Institute for Biological Standards and Control NIBSC, and WHO provided vaccine developers and the entire scientific community with a research reagent for an anti-SARS-CoV-2 antibody. The availability of this material was crucial for facilitating the development of diagnostics, vaccines, and therapeutic preparations. This effort was an initial response when NIBSC, in its capacity as a WHO collaborating centre, was working on the preparation of the WHO International Standards. This work included a collaborative study that was launched in July, 2020, to test serum samples and plasma samples sourced from convalescent patients with the aim of selecting the most suitable candidate material for the WHO International Standards for anti-SARS-CoV-2 immunoglobulin. The study involved 44 laboratories from 15 countries and the use of live and pseudotype-based neutralisation assays, ELISA, rapid tests, and other methods. The outcomes of the study were submitted to WHO in November, 2020. The inter-laboratory variation was reduced more than 50 times for neutralisation and 2000 times for ELISA when assay values were reported relative to the International International Standard and International Reference Panel for anti-SARS-CoV-2 immunoglobulins were adopted by the WHO Expert Committee on Biological Standardization on Dec 10, WHO International Standard for anti-SARS-CoV-2 Scholar The International Standard allows the accurate calibration of assays to an arbitrary unit, thereby reducing inter-laboratory variation and creating a common language for reporting data. The International Standard is based on pooled human plasma from convalescent patients, which is lyophilised in ampoules, with an assigned unit of 250 international units IU per ampoule for neutralising activity. For binding assays, a unit of 1000 binding antibody units BAU per mL can be used to assist the comparison of assays detecting the same class of immunoglobulins with the same specificity eg, anti-receptor-binding domain IgG, anti-N IgM, etc The International Standard is available in the NIBSC have been launched for the harmonisation of immune response assessment across COVID-19 vaccine candidates, including the CEPI Global Centralised Laboratory for Epidemic Preparedness InnovationsCEPI establishes global network of laboratories to centralise assessment of COVID-19 vaccine Scholar CEPI centralised laboratories will achieve harmonisation of the results from different vaccine clinical trials with the use of common standard operating procedures and the same crucial reagents, including a working standard calibrated to the international basic tool for any harmonisation is the global use of an International Standard and IU to which assay data need to be calibrated with the use of a reliable method. It is therefore crucial that the International Standard is properly used by all vaccine developers, national reference laboratories, and academic groups worldwide, and that immunogenicity results are reported as an international standard unit IU/mL for neutralising antibodies and BAU/mL for binding assay formats.In this manner, the results from clinical trials expressed in IU would allow for the comparison of the immune responses after natural infection and induced by various vaccine candidates. This comparison is particularly important for the identification of correlates of protection against COVID-19; should neutralising antibodies be further supported as a component of the protective response, the expression of antibody responses in IU/mL is essential to gather a consensus from several clinical trials and other studies on the titre required for the correlate of protection against SARS-2-CoV has not yet been unequivocally defined, antibodies are likely to be at least part of the protective response. The effect of new variants on the evaluation of antibodies is obvious and unequivocal comparisons are required. Reporting the immunological responses from vaccine clinical trials against the International Standard is essential for the evaluation of clinical data submitted to national regulatory authorities as well as to WHO for emergency use listing, especially as placebo-controlled efficacy studies become operationally unfeasible. There will be a substantial effect on the use of the International Standard if regulatory authorities worldwide request data in IU/mL or BAU/mL. We also encourage journal editors and peer reviewers to ensure that the international standard is used as the benchmark in publications and that data from serology assays are reported in International Standard declare no competing TT Cramer JP Chen R Mayhew S Evolution of the COVID-19 vaccine development Rev Drug Discov. 2020; 19 WHO International Standard for anti-SARS-CoV-2 for Epidemic Preparedness InnovationsCEPI establishes global network of laboratories to centralise assessment of COVID-19 vaccine infoPublication historyPublished March 23, 2021IdentificationDOI Copyright © 2021 Published by Elsevier Ltd. All rights this article on ScienceDirectView Large ImageDownload Hi-res image Download .PPT

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