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Publication Abstract from PubMed

SARS-CoV-2 is one of three coronaviruses that have crossed the animal-to-human barrier and caused widespread disease in the past two decades. The development of a universal human coronavirus vaccine could prevent future pandemics. We characterize 198 antibodies isolated from four COVID-19+ subjects and identify 14 SARS-CoV-2 neutralizing antibodies. One targets the N-terminal domain (NTD), one recognizes an epitope in S2, and 11 bind the receptor-binding domain (RBD). Three anti-RBD neutralizing antibodies cross-neutralize SARS-CoV-1 by effectively blocking binding of both the SARS-CoV-1 and SARS-CoV-2 RBDs to the ACE2 receptor. Using the K18-hACE transgenic mouse model, we demonstrate that the neutralization potency and antibody epitope specificity regulates the in vivo protective potential of anti-SARS-CoV-2 antibodies. All four cross-neutralizing antibodies neutralize the B.1.351 mutant strain. Thus, our study reveals that epitopes in S2 can serve as blueprints for the design of immunogens capable of eliciting cross-neutralizing coronavirus antibodies.

Isolation and characterization of cross-neutralizing coronavirus antibodies from COVID-19+ subjects.,Jennewein MF, MacCamy AJ, Akins NR, Feng J, Homad LJ, Hurlburt NK, Seydoux E, Wan YH, Stuart AB, Edara VV, Floyd K, Vanderheiden A, Mascola JR, Doria-Rose N, Wang L, Yang ES, Chu HY, Torres JL, Ozorowski G, Ward AB, Whaley RE, Cohen KW, Pancera M, McElrath MJ, Englund JA, Finzi A, Suthar MS, McGuire AT, Stamatatos L Cell Rep. 2021 Jul 13;36(2):109353. doi: 10.1016/j.celrep.2021.109353. Epub 2021 , Jun 22. PMID:34237283^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.