Diversity in glycosaminoglycan binding amongst hMPV G protein lineages.

摘要: We 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 interaction. GAG-dependent infectivity of available strains was demonstrated using GAG-deficient cells heparin competition. expressed the ectodomains from all analysed these by affinity chromatography. contrast to B2 lineage, neither or proteins bound heparin. Sequence analysis indicated although there some homology heparin-binding domains, were less positively charged residues, providing a likely explanation lack binding. Although sequence did not demonstrate well defined domains in A1 strain, able bind heparin, albeit lower than strain. These results indicate diversity GAG interactions between different lineages suggest GAG-dependency may be mediated interaction an alternative surface protein, most probably conserved fusion (F) protein. Analysis both native recombinant F confirmed binds supporting conclusion.