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Updated: May 20, 2025

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin
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Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin

Published on: March 10, 2021

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Structures of HCoV-OC43 HR1 Domain in Complex with Cognate HR2 or Analogue EK1 Peptide

Xiuxiu He1,2,3, Huanzhen Liu2, Guang Yang1,2,3

  • 1School of Food Science and Pharmaceutical Engineering, Nanjing Normal University, Nanjing 210023, China.

Viruses
|March 27, 2025
PubMed

Insights

Researchers elucidated the structure of the human coronavirus OC43 (HCoV-OC43) spike (S) protein

Area of Science:

  • Structural Biology
  • Virology
  • Molecular Biology

Background:

  • Human coronavirus OC43 (HCoV-OC43) causes common colds and severe illness in vulnerable populations.
  • The spike (S) glycoprotein of HCoV-OC43 mediates host-cell attachment and membrane fusion.

Purpose of the Study:

  • To determine the molecular mechanism of HCoV-OC43 membrane fusion.
  • To understand the structural basis for HCoV-OC43 S protein function.

Main Methods:

  • Crystal structure determination of the HCoV-OC43 S protein post-fusion core at 3.34 Å resolution.
  • Crystal structure determination of the HCoV-OC43 HR1P and fusion inhibitor EK1 complex at 2.71 Å resolution.

Main Results:

  • The post-fusion structure reveals a parallel trimeric coiled coil of HR1 helices with entwined HR2 helices.
  • The fusion inhibitor EK1, derived from HR2P, maintains key interactions within the fusion core, stabilizing its conformation.
  • Structural insights explain the mechanism of HCoV-OC43 S protein-mediated membrane fusion.

Conclusions:

  • The study reveals critical intrahelical and interhelical interactions in HCoV-OC43 S protein fusion.
  • Findings provide a mechanistic understanding of HCoV-OC43 inhibition by HR2 mimic peptides like EK1.

Keywords:
HCoV-OC43fusion corefusion inhibitor EK1heptad repeatsviral entry

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