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Mapping SARS-CoV-2 Antibody Epitopes in COVID-19 Patients with a Multi-Coronavirus Protein Microarray.
Microbiol Spectr. 2021 10 31; 9(2):e0141621.MS

Abstract

The rapid worldwide spread of SARS-CoV-2 has accelerated research and development for controlling the COVID-19 pandemic. A multi-coronavirus protein microarray was created containing full-length proteins, overlapping protein fragments of various lengths, and peptide libraries from SARS-CoV-2 and four other human coronaviruses. Sera from confirmed COVID-19 patients as well as unexposed individuals were applied to multicoronavirus arrays to identify specific antibody reactivity. High-level IgG, IgM, and IgA reactivity to structural proteins S, M, and N of SARS-CoV-2, as well as accessory proteins such as ORF3a and ORF7a, were observed that were specific to COVID-19 patients. Antibody reactivity against overlapping 100-, 50-, and 30-amino acid fragments of SARS-CoV-2 proteins was used to identify antigenic regions. Numerous proteins of SARS-CoV, Middle East respiratory syndrome coronavirus (MERS-CoV), and the endemic human coronaviruses HCoV-NL63 and HCoV-OC43 were also more reactive with IgG, IgM, and IgA in COVID-19 patient sera than in unexposed control sera, providing further evidence of immunologic cross-reactivity between these viruses. Whereas unexposed individuals had minimal reactivity against SARS-CoV-2 proteins that poorly correlated with reactivity against HCoV-NL63 and HCoV-OC43 S2 and N proteins, COVID-19 patient sera had higher correlation between SARS-CoV-2 and HCoV responses, suggesting that de novo antibodies against SARS-CoV-2 cross-react with HCoV epitopes. Array responses were compared with validated spike protein-specific IgG enzyme-linked immunosorbent assays (ELISAs), showing agreement between orthologous methods. SARS-CoV-2 microneutralization titers were low in the COVID-19 patient sera but correlated with array responses against S and N proteins. The multi-coronavirus protein microarray is a useful tool for mapping antibody reactivity in COVID-19 patients. IMPORTANCE With novel mutant SARS-CoV-2 variants of concern on the rise, knowledge of immune specificities against SARS-CoV-2 proteins is increasingly important for understanding the impact of structural changes in antibody-reactive protein epitopes on naturally acquired and vaccine-induced immunity, as well as broader topics of cross-reactivity and viral evolution. A multi-coronavirus protein microarray used to map the binding of COVID-19 patient antibodies to SARS-CoV-2 proteins and protein fragments as well as to the proteins of four other coronaviruses that infect humans has shown specific regions of SARS-CoV-2 proteins that are highly reactive with patient antibodies and revealed cross-reactivity of these antibodies with other human coronaviruses. These data and the multi-coronavirus protein microarray tool will help guide further studies of the antibody response to COVID-19 and to vaccination against this worldwide pandemic.

Authors+Show Affiliations

Antigen Discovery Incorporated (ADI), Irvine, California, USA. University of California, Irvine, California, USA.Antigen Discovery Incorporated (ADI), Irvine, California, USA.Antigen Discovery Incorporated (ADI), Irvine, California, USA.Antigen Discovery Incorporated (ADI), Irvine, California, USA.Antigen Discovery Incorporated (ADI), Irvine, California, USA.Antigen Discovery Incorporated (ADI), Irvine, California, USA.Antigen Discovery Incorporated (ADI), Irvine, California, USA.Antigen Discovery Incorporated (ADI), Irvine, California, USA.Antigen Discovery Incorporated (ADI), Irvine, California, USA.Antigen Discovery Incorporated (ADI), Irvine, California, USA.Antigen Discovery Incorporated (ADI), Irvine, California, USA.Centers for Disease Control and Preventiongrid.416738.f, Atlanta, Georgia, USA.Centers for Disease Control and Preventiongrid.416738.f, Atlanta, Georgia, USA.Centers for Disease Control and Preventiongrid.416738.f, Atlanta, Georgia, USA.Centers for Disease Control and Preventiongrid.416738.f, Atlanta, Georgia, USA.Centers for Disease Control and Preventiongrid.416738.f, Atlanta, Georgia, USA.Centers for Disease Control and Preventiongrid.416738.f, Atlanta, Georgia, USA.Centers for Disease Control and Preventiongrid.416738.f, Atlanta, Georgia, USA.Antigen Discovery Incorporated (ADI), Irvine, California, USA.Mayo Clinicgrid.66875.3a, Rochester, Minnesota, USA.Antigen Discovery Incorporated (ADI), Irvine, California, USA.Centers for Disease Control and Preventiongrid.416738.f, Atlanta, Georgia, USA.Antigen Discovery Incorporated (ADI), Irvine, California, USA.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

34704808

Citation

Camerini, David, et al. "Mapping SARS-CoV-2 Antibody Epitopes in COVID-19 Patients With a Multi-Coronavirus Protein Microarray." Microbiology Spectrum, vol. 9, no. 2, 2021, pp. e0141621.
Camerini D, Randall AZ, Trappl-Kimmons K, et al. Mapping SARS-CoV-2 Antibody Epitopes in COVID-19 Patients with a Multi-Coronavirus Protein Microarray. Microbiol Spectr. 2021;9(2):e0141621.
Camerini, D., Randall, A. Z., Trappl-Kimmons, K., Oberai, A., Hung, C., Edgar, J., Shandling, A., Huynh, V., Teng, A. A., Hermanson, G., Pablo, J. V., Stumpf, M. M., Lester, S. N., Harcourt, J., Tamin, A., Rasheed, M., Thornburg, N. J., Satheshkumar, P. S., Liang, X., ... Campo, J. J. (2021). Mapping SARS-CoV-2 Antibody Epitopes in COVID-19 Patients with a Multi-Coronavirus Protein Microarray. Microbiology Spectrum, 9(2), e0141621. https://doi.org/10.1128/Spectrum.01416-21
Camerini D, et al. Mapping SARS-CoV-2 Antibody Epitopes in COVID-19 Patients With a Multi-Coronavirus Protein Microarray. Microbiol Spectr. 2021 10 31;9(2):e0141621. PubMed PMID: 34704808.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Mapping SARS-CoV-2 Antibody Epitopes in COVID-19 Patients with a Multi-Coronavirus Protein Microarray. AU - Camerini,David, AU - Randall,Arlo Z, AU - Trappl-Kimmons,Krista, AU - Oberai,Amit, AU - Hung,Christopher, AU - Edgar,Joshua, AU - Shandling,Adam, AU - Huynh,Vu, AU - Teng,Andy A, AU - Hermanson,Gary, AU - Pablo,Jozelyn V, AU - Stumpf,Megan M, AU - Lester,Sandra N, AU - Harcourt,Jennifer, AU - Tamin,Azaibi, AU - Rasheed,Mohammed, AU - Thornburg,Natalie J, AU - Satheshkumar,Panayampalli S, AU - Liang,Xiaowu, AU - Kennedy,Richard B, AU - Yee,Angela, AU - Townsend,Michael, AU - Campo,Joseph J, Y1 - 2021/10/27/ PY - 2021/10/28/pubmed PY - 2021/11/17/medline PY - 2021/10/27/entrez KW - COVID-19 KW - HCoV KW - SARS-CoV-2 KW - antibody binding sites SP - e0141621 EP - e0141621 JF - Microbiology spectrum JO - Microbiol Spectr VL - 9 IS - 2 N2 - The rapid worldwide spread of SARS-CoV-2 has accelerated research and development for controlling the COVID-19 pandemic. A multi-coronavirus protein microarray was created containing full-length proteins, overlapping protein fragments of various lengths, and peptide libraries from SARS-CoV-2 and four other human coronaviruses. Sera from confirmed COVID-19 patients as well as unexposed individuals were applied to multicoronavirus arrays to identify specific antibody reactivity. High-level IgG, IgM, and IgA reactivity to structural proteins S, M, and N of SARS-CoV-2, as well as accessory proteins such as ORF3a and ORF7a, were observed that were specific to COVID-19 patients. Antibody reactivity against overlapping 100-, 50-, and 30-amino acid fragments of SARS-CoV-2 proteins was used to identify antigenic regions. Numerous proteins of SARS-CoV, Middle East respiratory syndrome coronavirus (MERS-CoV), and the endemic human coronaviruses HCoV-NL63 and HCoV-OC43 were also more reactive with IgG, IgM, and IgA in COVID-19 patient sera than in unexposed control sera, providing further evidence of immunologic cross-reactivity between these viruses. Whereas unexposed individuals had minimal reactivity against SARS-CoV-2 proteins that poorly correlated with reactivity against HCoV-NL63 and HCoV-OC43 S2 and N proteins, COVID-19 patient sera had higher correlation between SARS-CoV-2 and HCoV responses, suggesting that de novo antibodies against SARS-CoV-2 cross-react with HCoV epitopes. Array responses were compared with validated spike protein-specific IgG enzyme-linked immunosorbent assays (ELISAs), showing agreement between orthologous methods. SARS-CoV-2 microneutralization titers were low in the COVID-19 patient sera but correlated with array responses against S and N proteins. The multi-coronavirus protein microarray is a useful tool for mapping antibody reactivity in COVID-19 patients. IMPORTANCE With novel mutant SARS-CoV-2 variants of concern on the rise, knowledge of immune specificities against SARS-CoV-2 proteins is increasingly important for understanding the impact of structural changes in antibody-reactive protein epitopes on naturally acquired and vaccine-induced immunity, as well as broader topics of cross-reactivity and viral evolution. A multi-coronavirus protein microarray used to map the binding of COVID-19 patient antibodies to SARS-CoV-2 proteins and protein fragments as well as to the proteins of four other coronaviruses that infect humans has shown specific regions of SARS-CoV-2 proteins that are highly reactive with patient antibodies and revealed cross-reactivity of these antibodies with other human coronaviruses. These data and the multi-coronavirus protein microarray tool will help guide further studies of the antibody response to COVID-19 and to vaccination against this worldwide pandemic. SN - 2165-0497 UR - https://www.unboundmedicine.com/medline/citation/34704808/Mapping_SARS_CoV_2_Antibody_Epitopes_in_COVID_19_Patients_with_a_Multi_Coronavirus_Protein_Microarray_ L2 - https://doi.org/10.1128/Spectrum.01416-21 DB - PRIME DP - Unbound Medicine ER -