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Diversity in glycosaminoglycan binding amongst hMPV G protein lineages

Penelope Adamson1, Sutthiwan Thammawat, Gamaliel Muchondo

  • 1Department of Microbiology and Infectious Diseases, Flinders University, Flinders Medical Centre, Bedford Park, SA 5042, Australia. penelope.adamson@health.sa.gov.au

Viruses
|December 18, 2012
PubMed

Insights

Human metapneumovirus (hMPV) G protein interactions with glycosaminoglycans (GAGs) vary by subtype. While some strains show GAG-dependent infectivity, the fusion (F) protein likely mediates this interaction across all hMPV strains.

Area of Science:

  • Virology
  • Molecular Biology
  • Cell Biology

Background:

  • Human metapneumovirus (hMPV) is a significant respiratory pathogen.
  • Previous studies demonstrated GAG-binding by the hMPV G protein of the B2 lineage.

Purpose of the Study:

  • To investigate glycosaminoglycan (GAG) interactions of hMPV G proteins from A1, A2, and B1 subtypes.
  • To explore the role of the hMPV fusion (F) protein in GAG-dependent infectivity.

Main Methods:

  • GAG-dependent infectivity assays using GAG-deficient cells and heparin competition.
  • Heparin affinity chromatography of expressed G protein ectodomains.
  • Sequence analysis of G protein strains.
  • Analysis of native and recombinant F protein for heparin binding.

Main Results:

  • hMPV G proteins from A2 and B1 subtypes did not bind heparin, unlike the B2 lineage.
  • Sequence analysis revealed fewer positively charged residues in A2 and B1 G proteins, explaining the lack of binding.
  • The A1 G protein bound heparin with lower affinity.
  • Both native and recombinant F proteins were confirmed to bind heparin.

Conclusions:

  • Significant diversity exists in GAG interactions among different hMPV G protein lineages.
  • The conserved fusion (F) protein likely mediates GAG-dependency for all hMPV strains, not solely the G protein.
  • Findings suggest potential therapeutic targets by understanding these protein-GAG interactions.

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