4h32

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The crystal structure of the hemagglutinin H17 derived the bat influenza A virus

Structural highlights

4h32 is a 12 chain structure with sequence from Influenza A virus (A/little yellow-shouldered bat/Guatemala/060/2010(H17N10)). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.7Å
Ligands:NAG
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

H6QM93_9INFA 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

A new influenza-like virus genome (H17N10) was recently discovered in bats and offers a new perspective about the origin and evolution of influenza viruses. The viral envelope glycoprotein hemagglutinin (HA) is responsible for influenza virus receptor binding, fusion, and entry into the cell; therefore, the structure and function of HA H17 was characterized. The 2.70 A resolution crystal structure revealed that H17 has a typical influenza A virus HA fold, but with some special features, including a distorted putative sialic acid (SA) binding site and low thermostability. No binding to either the canonical human alpha2,6 SA-linkage or avian alpha2,3 SA-linkage receptor was observed. Furthermore, H17 glycan binding was not detected using a chip covering more than 600 glycans. Our results demonstrate that H17 is unique among characterized HAs and that the bat-derived influenza virus may use a different entry mechanism compared to canonical influenza viruses.

Bat-derived influenza hemagglutinin H17 does not bind canonical avian or human receptors and most likely uses a unique entry mechanism.,Sun X, Shi Y, Lu X, He J, Gao F, Yan J, Qi J, Gao GF Cell Rep. 2013 Mar 28;3(3):769-78. doi: 10.1016/j.celrep.2013.01.025. Epub 2013, Feb 21. PMID:23434510[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
22 reviews cite this structure
Bat-derived influenza-like viruses H17N10 and H18N11.
Wu et al. (2014)
21 more
50 other articles
No citations found

See Also

References

  1. ↑ Sun X, Shi Y, Lu X, He J, Gao F, Yan J, Qi J, Gao GF. Bat-derived influenza hemagglutinin H17 does not bind canonical avian or human receptors and most likely uses a unique entry mechanism. Cell Rep. 2013 Mar 28;3(3):769-78. doi: 10.1016/j.celrep.2013.01.025. Epub 2013, Feb 21. PMID:23434510 doi:10.1016/j.celrep.2013.01.025

Contents


PDB ID 4h32

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OCA

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