Structural highlights
Publication Abstract from PubMed
Influenza A and B viruses are responsible for the severe morbidity and mortality worldwide in annual influenza epidemics. Currently circulating influenza B virus belongs to the B/Victoria or B/Yamagata lineage that was diverged from each other about 30-40 years ago. However, a mechanistic understanding of their divergent evolution is still lacking. Here we report the crystal structures of influenza B/Yamanashi/166/1998 hemagglutinin (HA) belonging to B/Yamagata lineage and its complex with the avian-like receptor analogue. Comparison of these structures with those of undiverged and diverged influenza B virus HAs, in conjunction with sequence analysis, reveals the molecular basis for the divergent evolution of influenza B virus HAs. Furthermore, HAs of diverged influenza B virus strains display much stronger molecular interactions with terminal sialic acid of bound receptors, which may allow for a different tissue tropism for current influenza B viruses, for which further investigation is required.
Structural basis for the divergent evolution of influenza B virus hemagglutinin.,Ni F, Kondrashkina E, Wang Q Virology. 2013 Nov;446(1-2):112-22. doi: 10.1016/j.virol.2013.07.035. Epub 2013, Aug 27. PMID:24074573[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ni F, Kondrashkina E, Wang Q. Structural basis for the divergent evolution of influenza B virus hemagglutinin. Virology. 2013 Nov;446(1-2):112-22. doi: 10.1016/j.virol.2013.07.035. Epub 2013, Aug 27. PMID:24074573 doi:http://dx.doi.org/10.1016/j.virol.2013.07.035