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Dynamics of Neutralizing Antibodies and Binding Antibodies to Domains of SARS-CoV-2 Spike Protein in COVID-19 Survivors
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Metadata
Document Title
Dynamics of Neutralizing Antibodies and Binding Antibodies to Domains of SARS-CoV-2 Spike Protein in COVID-19 Survivors
Author
Phakaratsakul S, Manopwisedjaroen S, Boonarkart C, Kupatawintu P, Chaiwanichsiri D, Roytrakul T, Auewarakul P, Thitithanyanont A
Name from Authors Collection
Affiliations
Mahidol University; Mahidol University; Thai Red Cross Society; National Science & Technology Development Agency - Thailand; National Center Genetic Engineering & Biotechnology (BIOTEC); Mahidol University; Mahidol University
Type
Article; Early Access
Source Title
VIRAL IMMUNOLOGY
ISSN
0882-8245
Page
-
Open Access
Green Submitted
Publisher
MARY ANN LIEBERT, INC
DOI
10.1089/vim.2022.0059
Format
Abstract
Neutralizing antibody level is used to predict immune protection against SARS-CoV-2 infection. Spike protein of SARS-CoV-2 is a major target for virus-neutralizing antibody. A number of neutralizing epitopes were mapped on receptor binding domain (RBD) and N-terminal domain (NTD) of S1 subunit of the spike. Anti-SARS-CoV-2 antibody usually decreases over time after recovery. Level of neutralizing antibody and binding antibody to several domains from COVID-19 recovered patients was observed longitudinally in this study. Sequentially collected serum samples from 35 patients demonstrated both similar and different trends of neutralizing antibodies versus binding antibodies to each domain. Twenty-three individuals showed similarly decreasing pattern of neutralizing titer, binding antibodies to RBD, NTD, fusion protein (S2), and nucleocapsid (NP). Interestingly, eight individuals had stably high neutralizing titer (>= 320) for 3-12 months, whereas their binding antibodies to RBD, NTD, and NP rapidly decreased. Moreover, their binding antibodies to S2 were stable over time similar to the persistence of neutralizing antibody levels. The long-lasting antibody to S2 suggested an anamnestic response to cross-reactive epitopes from previous infections with other related coronaviruses. These data indicate a difference in kinetics and longevity of antibodies to various domains and epitopes of the SARS-CoV-2 proteins. A better understanding in this difference may help improve vaccine design to induce long-lasting immunity to COVID-19.
Funding Sponsor
National Science andTechnology Development Agency, Thailand [P-20-50640]; Faculty of Medicine Siriraj Hospital, Mahidol University, Thailand
License
CC BY
Rights
Mary Ann Liebert, Inc., publishers
Publication Source
WOS