In:
PLOS ONE, Public Library of Science (PLoS), Vol. 17, No. 4 ( 2022-4-18), p. e0264723-
Abstract:
The serine proteases neutrophil elastase (NE), proteinase 3 (PR3), cathepsin G (CatG), and neutrophil serine protease 4 (NSP4) are secreted by activated neutrophils as a part of the innate immune response against invading pathogens. However, these serine proteases might be adopted by viruses to mediate viral surface protein priming resulting in host cell entrance and productive infection. Indeed, NE and PR3 hydrolyze the scissile peptide bond within the proteolytically sensitive polybasic sequence of the activation loop of SARS-CoV-2 located at the S1/S2 interface of the Spike (S) protein; an amino acid motif which differs from SARS-CoV-1. The occurrence of novel SARS-CoV-2 variants and substitution of distinct amino acids at the polybasic sequence prompts serious concerns regarding increased transmissibility. We propose that a novel cleavage site by CatG of the Omicron variant and the increased substrate turnover of the Delta variant by furin within the polybasic sequence should be considered for increased transmission of SARS-CoV-2 variants.
Type of Medium:
Online Resource
ISSN:
1932-6203
DOI:
10.1371/journal.pone.0264723
DOI:
10.1371/journal.pone.0264723.g001
DOI:
10.1371/journal.pone.0264723.g002
DOI:
10.1371/journal.pone.0264723.g003
DOI:
10.1371/journal.pone.0264723.g004
DOI:
10.1371/journal.pone.0264723.s001
DOI:
10.1371/journal.pone.0264723.s002
DOI:
10.1371/journal.pone.0264723.s003
DOI:
10.1371/journal.pone.0264723.s004
DOI:
10.1371/journal.pone.0264723.s005
Language:
English
Publisher:
Public Library of Science (PLoS)
Publication Date:
2022
detail.hit.zdb_id:
2267670-3
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