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MERS-CoV and SARS-CoV-2 membrane proteins are modified with polylactosamine chains

Dylan Juckel1, Lowiese Desmarets1, Adeline Danneels1

  • 1Univ. Lille, CNRS, Inserm, CHU Lille, Institut Pasteur de Lille, U1019 - UMR 9017 - CIIL- Center for Infection and Immunity of Lille, F-59000 Lille, France.

The Journal of General Virology
|October 6, 2023
PubMed

Insights

The M protein of SARS-CoV-2 and MERS-CoV undergoes polylactosamine glycosylation, a process requiring specific acidic residues. This finding sheds light on coronavirus assembly and potential therapeutic targets.

Area of Science:

  • Virology
  • Molecular Biology
  • Glycobiology

Background:

  • Coronaviruses are enveloped viruses with key structural proteins including Spike (S), Membrane (M), and Envelope (E).
  • The M protein is crucial for viral envelope formation and integrity.
  • MERS-CoV and SARS-CoV-2 M proteins possess an N-glycosylation site.

Purpose of the Study:

  • To investigate the N-glycosylation of MERS-CoV and SARS-CoV-2 M proteins.
  • To identify the specific type of glycosylation and the cellular requirements for this modification.

Main Methods:

  • Transfection and infection of cells with MERS-CoV and SARS-CoV-2.
  • Analysis of M protein glycosylation patterns.
  • Site-directed mutagenesis to identify key residues for glycosylation.

Main Results:

  • Polylactosamine chains are conjugated to MERS-CoV and SARS-CoV-2 M proteins in both transfected and infected cells.
  • Acidic residues within the first transmembrane segments are essential for M protein glycosylation.
  • No specific signal for polylactosamine conjugation was identified; high mannose-conjugated protein was observed in virus-like particles.

Conclusions:

  • The M protein of SARS-CoV-2 and MERS-CoV undergoes specific N-glycosylation with polylactosamine chains.
  • Acidic residues in transmembrane segments are critical for this glycosylation process.
  • Understanding M protein glycosylation may offer insights into coronavirus assembly and host-pathogen interactions.
Keywords:
N-linked glycosylationcoronavirusmembrane proteinpolylactosamines

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