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Oligomerization-Dependent Beta-Structure Formation in SARS-CoV-2 Envelope Protein.

Wahyu Surya1, Jaume Torres1

  • 1School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, Singapore.

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|November 11, 2022
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Summary

SARS-CoV-2 E protein forms beta-structures in ERGIC-like membranes, triggered by monomer interactions. This structure may influence viral assembly and channel activity.

Keywords:
Fourier-transform infrared spectroscopySARS-CoV-2analytical ultracentrifugationconformational changeenvelope proteinion channelscission mechanism

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Area of Science:

  • Structural Biology
  • Virology
  • Membrane Biophysics

Background:

  • The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) causes the COVID-19 pandemic.
  • The SARS-CoV-2 envelope (E) protein forms channels and is crucial for viral replication.
  • Previous studies on E protein extramembrane domains yielded models lacking beta-strands, contradicting predictions.

Purpose of the Study:

  • To investigate the conformation of SARS-CoV-2 E protein within lipid bilayers mimicking ER-Golgi intermediate compartment (ERGIC) membranes.
  • To determine the structural changes of the E protein in response to protein concentration and membrane environment.

Main Methods:

  • Purified SARS-CoV-2 E protein was studied in model lipid bilayers (POPC:POPG).
  • Fourier-transform infrared spectroscopy (FTIR) was used to analyze protein secondary structure.
  • Experiments were conducted at varying protein-to-lipid ratios and with a truncated E protein variant.

Main Results:

  • High concentrations of full-length E protein in lipid bilayers induced beta-structure formation (peak at 1635 cm⁻¹).
  • Lower concentrations or truncated E protein showed predominantly beta-turns (peak at 1688 cm⁻¹).
  • Monomer-monomer interactions were identified as the trigger for beta-structure formation in the C-terminal extramembrane domain.

Conclusions:

  • SARS-CoV-2 E protein undergoes a conformational change to a beta-structure in ERGIC-like membranes, dependent on protein concentration and oligomerization.
  • This concentration-dependent structural transition, involving the C-terminal extramembrane domain, may regulate E protein channel activity.
  • The findings suggest a mechanism by which the E protein influences membrane structure during virion formation.