Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 574, Issue -, Pages 14-19Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2021.08.036
Keywords
SARS-CoV-2 variants; Delta variant B; 1; 617; 2; Molecular dynamics; Immune escape; Antibody binding
Categories
Funding
- National Science Foundation [2037374]
- University Graduate School at Florida International University
- Division Of Computer and Network Systems
- Direct For Computer & Info Scie & Enginr [2037374] Funding Source: National Science Foundation
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The surges of the more infectious Delta variant have intensified the health crisis, but current vaccines offer protection against it. However, the Delta variant can evade the immune system to some extent by reducing the receptivity of neutralizing antibodies.
Following the initial surges of the Alpha (B.1.1.7) and the Beta (B.1.351) variants, a more infectious Delta variant (B.1.617.2) is now surging, further deepening the health crises caused by the pandemic. The sharp rise in cases attributed to the Delta variant has made it especially disturbing and is a variant of concern. Fortunately, current vaccines offer protection against known variants of concern, including the Delta variant. However, the Delta variant has exhibited some ability to dodge the immune system as it is found that neutralizing antibodies from prior infections or vaccines are less receptive to binding with the Delta spike protein. Here, we investigated the structural changes caused by the mutations in the Delta variant's receptor-binding interface and explored the effects on binding with the ACE2 receptor as well as with neutralizing antibodies. We find that the receptor-binding b-loop -b motif adopts an altered but stable conformation causing separation in some of the antibody binding epitopes. Our study shows reduced binding of neutralizing antibodies and provides a possible mechanism for the immune evasion exhibited by the Delta variant. (c) 2021 Elsevier Inc. All rights reserved.
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