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Ross River virus envelope glycans contribute to disease through activation of the host complement system

Bronwyn M Gunn1, Jennifer E Jones1, Reed S Shabman1

  • 1Dept. of Microbiology and Immunology, University of North Carolina at Chapel Hill, 160 Dental Circle, 9024 Burnett Womack, Chapel Hill, NC 27599, USA.

Virology
|January 12, 2018
PubMed

Insights

Mannose-binding lectin (MBL) can worsen Ross River virus (RRV) disease. Viral N-linked glycans promote MBL binding, leading to inflammation and tissue damage, contributing to arthritis and myositis.

Area of Science:

  • Virology
  • Immunology
  • Glycobiology

Background:

  • Mannose-binding lectin (MBL) typically protects against viral infections.
  • However, MBL-mediated complement activation can exacerbate Ross River virus (RRV)-induced inflammatory conditions like arthritis and myositis.

Purpose of the Study:

  • To investigate if N-linked glycans on RRV envelope glycoproteins serve as ligands for MBL.
  • To determine the role of these glycans in MBL deposition, complement activation, and disease pathogenesis.

Main Methods:

  • Utilized RRV mutants lacking N-linked glycans on envelope glycoproteins.
  • Assessed MBL deposition on infected cells.
  • Evaluated disease severity and tissue damage in a mouse model of RRV-induced myositis.
  • Measured viral load and inflammatory infiltrates.

Main Results:

  • MBL deposition onto RRV-infected cells was dependent on E2 envelope glycans.
  • Glycan-deficient RRV mutants showed reduced disease and tissue damage in mice.
  • This reduction was associated with decreased MBL deposition and complement activation, despite similar viral loads.

Conclusions:

  • Viral N-linked glycans act as ligands for MBL during RRV infection.
  • These glycans promote MBL deposition and subsequent complement activation.
  • This process contributes significantly to the development of RRV-induced myositis and tissue damage.
Keywords:
AlphavirusComplementMannose-binding lectinN-linked glycanRoss River virus

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