4M44

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

Summary for 4M44

• Entry DOI: 10.2210/pdb4m44/pdb
• Related: 4M40
• Descriptor: Hemagglutinin HA1, Hemagglutinin HA2, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• Functional Keywords: receptor binding, fusion, sialic acid, viral protein
• Biological source: Influenza B virus; More
• Total number of polymer chains: 6
• Total formula weight: 180242.41

Authors

Ni, F.,Kondrashkina, E.,Wang, Q. (deposition date: 2013-08-06, release date: 2013-09-25, Last modification date: 2020-07-29)

Primary citation

Ni, F.,Kondrashkina, E.,Wang, Q.
Structural basis for the divergent evolution of influenza B virus hemagglutinin.
Virology, 446:112-122, 2013

PubMed Abstract: 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.

PubMed: 24074573
DOI: 10.1016/j.virol.2013.07.035

Experimental method

X-RAY DIFFRACTION (2.5 Å)