Structural highlights
Publication Abstract from PubMed
Two ferret-adapted H5N1 viruses capable of respiratory droplet transmission have been reported with mutations in the hemagglutinin receptor-binding site and stalk domains. Glycan microarray analysis reveals that both viruses exhibit a strong shift towards binding to 'human-type' alpha2-6 sialosides, but with notable differences in fine specificity. Crystal structure analysis further shows that the stalk mutation causes no obvious perturbation of the receptor-binding pocket, consistent with its impact on hemagglutinin stability without effecting receptor specificity.
Hemagglutinin receptor specificity and structural analyses of respiratory droplet transmissible H5N1 viruses.,de Vries RP, Zhu X, McBride R, Rigter A, Hanson A, Zhong G, Hatta M, Xu R, Yu W, Kawaoka Y, de Haan CA, Wilson IA, Paulson JC J Virol. 2013 Oct 30. PMID:24173215[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ de Vries RP, Zhu X, McBride R, Rigter A, Hanson A, Zhong G, Hatta M, Xu R, Yu W, Kawaoka Y, de Haan CA, Wilson IA, Paulson JC. Hemagglutinin receptor specificity and structural analyses of respiratory droplet transmissible H5N1 viruses. J Virol. 2013 Oct 30. PMID:24173215 doi:http://dx.doi.org/10.1128/JVI.02690-13