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4wa1

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Revision as of 07:29, 27 September 2023 by OCA (Talk | contribs)

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The crystal structure of hemagglutinin from a H3N8 influenza virus isolated from New England harbor seals

Structural highlights

4wa1 is a 6 chain structure with sequence from Influenza A virus (A/harbor seal/Massachusetts/1/2011(H3N8)). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.898Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

I6NNE1_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.[RuleBase:RU003324][SAAS:SAAS00070610]

Publication Abstract from PubMed

In late 2011, an A(H3N8) influenza virus infection resulted in the deaths of 162 New England harbor seals. Virus sequence analysis and virus receptor binding studies highlighted potential markers responsible for mammalian adaptation and a mixed receptor binding preference (Anthony et al. ; MBio 3: e00166-00112). Here we present a detailed structural and biochemical analysis of the surface antigens of this virus. Results obtained with recombinant proteins for both the hemagglutinin and neuraminidase, indicate a true avian receptor binding preference. Although the detection of this virus in new species highlights an increased potential for cross-species transmission with these viruses, our results indicate that the A(H3N8) virus currently poses a low risk to humans. IMPORTANCE: Cross-species transmission of zoonotic influenza viruses increases public health concerns. Here we report a molecular and structural study of the major surface proteins from an A(H3N8) influenza virus isolated from New England harbor seals. Results improve our understanding of these viruses as they evolve and provide important information to aid ongoing risk assessment analyses, as these zoonotic influenza viruses continue to circulate and adapt to new hosts.

Structural and functional analysis of surface proteins from an A(H3N8) influenza virus isolated from New England harbor seals.,Yang H, Nguyen HT, Carney PJ, Guo Z, Chang JC, Jones J, Davis CT, Villanueva JM, Gubareva LV, Stevens J J Virol. 2014 Dec 24. pii: JVI.02723-14. PMID:25540377^[1]

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

References

↑ Yang H, Nguyen HT, Carney PJ, Guo Z, Chang JC, Jones J, Davis CT, Villanueva JM, Gubareva LV, Stevens J. Structural and functional analysis of surface proteins from an A(H3N8) influenza virus isolated from New England harbor seals. J Virol. 2014 Dec 24. pii: JVI.02723-14. PMID:25540377 doi:http://dx.doi.org/10.1128/JVI.02723-14