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Membrane fusion and immune evasion by the spike protein of SARS-CoV-2 Delta variant.

<div class='caption-title'>More efficient membrane fusion by the Delta variant than other variants.</div>
<div class='caption-title'>Antigenic properties of purified full-length SARS-CoV-2 S proteins.</div>
<div class='caption-title'>Cryo-EM structures of full-length SARS-CoV-2 S proteins from the Delta, Kappa, and Gamma variants.</div>
Zhang J, Xiao T, Cai Y, Lavine CL, Peng H, Zhu H, Anand K, Tong P, Gautam A, Mayer ML, Walsh RM, Rits-Volloch S, Wesemann DR, Yang W, Seaman MS, Lu J, Chen B, Chen B
OpenAccess logo Science 374 1353-1360 (2021)
Related entries: 7sbk, 7sbl, 7sbp, 7sbq, 7sbr, 7sbs, 7sbt

Cited: 182 times
EuropePMC logo PMID: 34698504

Abstract

The Delta variant of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has outcompeted previously prevalent variants and become a dominant strain worldwide. We report the structure, function, and antigenicity of its full-length spike (S) trimer as well as those of the Gamma and Kappa variants, and compare their characteristics with the G614, Alpha, and Beta variants. Delta S can fuse membranes more efficiently at low levels of cellular receptor angiotensin converting enzyme 2 (ACE2), and its pseudotyped viruses infect target cells substantially faster than the other five variants, possibly accounting for its heightened transmissibility. Each variant shows different rearrangement of the antigenic surface of the amino-terminal domain of the S protein but only makes produces changes in the receptor binding domain (RBD), making the RBD a better target for therapeutic antibodies.

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