Open AccessHCoV-229E spike protein fusion activation by trypsin-like serine proteases is mediated by proteolytic processing in the S2′ region
Author(s) -
Ariane Bonnin,
Adeline Danneels,
Jean Dubuisson,
Anne Goffard,
Sandrine Belouzard
Publication year - 2018
Publication title -
journal of general virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.55
H-Index - 167
eISSN - 1465-2099
pISSN - 0022-1317
DOI - 10.1099/jgv.0.001074
Subject(s) - proteases , trypsin , serine , biology , coronavirus , serine protease , microbiology and biotechnology , biochemistry , protease , enzyme , covid-19 , medicine , infectious disease (medical specialty) , disease , pathology
Human coronavirus 229E (HCoV-229E) is responsible for common colds. Like other coronaviruses, HCoV-229E exploits cellular proteases to activate fusion mediated by the spike protein. We analysed the proteolytic processing of the HCoV-229E spike protein by trypsin-like serine proteases leading to activation of the fusion process. Unlike in other coronaviruses, HCoV-229E fusion activation appears to be a one-step process. Indeed, cleavage of the S1/S2 interface does not seem to be a prerequisite, and the fusion activation is highly reliant on the S2' region, with arginine residue 683 acting as the recognition site.