In:
PLOS Pathogens, Public Library of Science (PLoS), Vol. 19, No. 5 ( 2023-5-17), p. e1011123-
Abstract:
SARS-CoV Spike (S) protein shares considerable homology with SARS-CoV-2 S, especially in the conserved S2 subunit (S2). S protein mediates coronavirus receptor binding and membrane fusion, and the latter activity can greatly influence coronavirus infection. We observed that SARS-CoV S is less effective in inducing membrane fusion compared with SARS-CoV-2 S. We identify that S813T mutation is sufficient in S2 interfering with the cleavage of SARS-CoV-2 S by TMPRSS2, reducing spike fusogenicity and pseudoparticle entry. Conversely, the mutation of T813S in SARS-CoV S increased fusion ability and viral replication. Our data suggested that residue 813 in the S was critical for the proteolytic activation, and the change from threonine to serine at 813 position might be an evolutionary feature adopted by SARS-2-related viruses. This finding deepened the understanding of Spike fusogenicity and could provide a new perspective for exploring Sarbecovirus ’ evolution.
Type of Medium:
Online Resource
ISSN:
1553-7374
DOI:
10.1371/journal.ppat.1011123
DOI:
10.1371/journal.ppat.1011123.g001
DOI:
10.1371/journal.ppat.1011123.g002
DOI:
10.1371/journal.ppat.1011123.g003
DOI:
10.1371/journal.ppat.1011123.g004
DOI:
10.1371/journal.ppat.1011123.g005
DOI:
10.1371/journal.ppat.1011123.g006
DOI:
10.1371/journal.ppat.1011123.g007
DOI:
10.1371/journal.ppat.1011123.s001
DOI:
10.1371/journal.ppat.1011123.s002
DOI:
10.1371/journal.ppat.1011123.s003
Language:
English
Publisher:
Public Library of Science (PLoS)
Publication Date:
2023
detail.hit.zdb_id:
2205412-1
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