Diversity in Glycosaminoglycan Binding Amongst hMPV G Protein Lineages
AbstractWe have previously shown that hMPV G protein (B2 lineage) interacts with cellular glycosaminoglycans (GAGs). In this study we examined subtypes A1, A2 and B1 for this interaction. GAG-dependent infectivity of available hMPV strains was demonstrated using GAG-deficient cells and heparin competition. We expressed the G protein ectodomains from all strains and analysed these by heparin affinity chromatography. In contrast to the B2 lineage, neither the A2 or B1 G proteins bound to heparin. Sequence analysis of these strains indicated that although there was some homology with the B2 heparin-binding domains, there were less positively charged residues, providing a likely explanation for the lack of binding. Although sequence analysis did not demonstrate well defined positively charged domains in G protein of the A1 strain, this protein was able to bind heparin, albeit with a lower affinity than G protein of the B2 strain. These results indicate diversity in GAG interactions between G proteins of different lineages and suggest that the GAG-dependency of all strains may be mediated by interaction with an alternative surface protein, most probably the conserved fusion (F) protein. Analysis of both native and recombinant F protein confirmed that F protein binds heparin, supporting this conclusion.
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Adamson, P.; Thammawat, S.; Muchondo, G.; Sadlon, T.; Gordon, D. Diversity in Glycosaminoglycan Binding Amongst hMPV G Protein Lineages. Viruses 2012, 4, 3785-3803.
Adamson P, Thammawat S, Muchondo G, Sadlon T, Gordon D. Diversity in Glycosaminoglycan Binding Amongst hMPV G Protein Lineages. Viruses. 2012; 4(12):3785-3803.Chicago/Turabian Style
Adamson, Penelope; Thammawat, Sutthiwan; Muchondo, Gamaliel; Sadlon, Tania; Gordon, David. 2012. "Diversity in Glycosaminoglycan Binding Amongst hMPV G Protein Lineages." Viruses 4, no. 12: 3785-3803.