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The receptor binding domain of SARS-CoV-2 spike is the key target of neutralizing antibody in human polyclonal sera.

Steffen, T.; Stone, E. T.; Hassert, M.; Geerling, E.; Grimberg, B. T.; Espino, A. M.; Pantoja, P.; Climent, C.; Hoft, D. F.; George, S. L.; Sariol, C. A.; Pinto, A. K.; Brien, J. D.

2020-08-22 immunology
10.1101/2020.08.21.261727 bioRxiv
Show abstract

Natural infection of SARS-CoV-2 in humans leads to the development of a strong neutralizing antibody response, however the immunodominant targets of the polyclonal neutralizing antibody response are still unknown. Here, we functionally define the role SARS-CoV-2 spike plays as a target of the human neutralizing antibody response. In this study, we identify the spike protein subunits that contain antigenic determinants and examine the neutralization capacity of polyclonal sera from a cohort of patients that tested qRT-PCR-positive for SARS-CoV-2. Using an ELISA format, we assessed binding of human sera to spike subunit 1 (S1), spike subunit 2 (S2) and the receptor binding domain (RBD) of spike. To functionally identify the key target of neutralizing antibody, we depleted sera of subunit-specific antibodies to determine the contribution of these individual subunits to the antigen-specific neutralizing antibody response. We show that epitopes within RBD are the target of a majority of the neutralizing antibodies in the human polyclonal antibody response. These data provide critical information for vaccine development and development of sensitive and specific serological testing.

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