HCoV-229E spike protein fusion activation by trypsin-like serine proteases is mediated by proteolytic processing in the S2' region

J Gen Virol. 2018 Jul;99(7):908-912. doi: 10.1099/jgv.0.001074. Epub 2018 May 22.

Abstract

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.

Keywords: HCoV-229E; entry; fusion; spike protein.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Coronavirus 229E, Human / chemistry
  • Coronavirus 229E, Human / genetics*
  • Coronavirus Infections
  • HEK293 Cells
  • Humans
  • Serine Endopeptidases / metabolism*
  • Spike Glycoprotein, Coronavirus / chemistry*
  • Spike Glycoprotein, Coronavirus / genetics
  • Viral Core Proteins / genetics*
  • Viral Fusion Proteins / chemistry*
  • Viral Fusion Proteins / genetics

Substances

  • Spike Glycoprotein, Coronavirus
  • Viral Core Proteins
  • Viral Fusion Proteins
  • trypsin-like serine protease
  • Serine Endopeptidases