4m44

From Proteopedia

Crystal structure of hemagglutinin of influenza virus B/Yamanashi/166/1998 in complex with avian-like receptor LSTa

Structural highlights

4m44 is a 6 chain structure with sequence from Influenza B virus (B/Yamanashi/166/1998). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.5Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A3DQM7_9INFB Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore (By similarity).[RuleBase:RU003324]

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.

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