Mapping SARS-CoV-2 Antibody Epitopes in COVID-19 Patients with a Multi-Coronavirus Protein Microarray
David Camerini, Arlo Randall, Krista Trappl-Kimmons, Amit Oberai, Christopher Hung, Joshua Edgar, Adam D. Shandling, Vu Huynh, Andy Teng, Gary Hermanson, Jozelyn Pablo, Megan M. Stumpf, Sandra Lester, Jennifer L. Harcourt, Azaibi Tamin, Mohammed Rasheed, Natalie J. Thornburg, Panayampalli S. Satheshkumar, Xiaowu Liang, Richard B. Kennedy, Angela Yee, Michael B. Townsend, Joseph J. Campo
Abstract
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.