Structural highlights
Function
[HEMA_I68A4] 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).
Publication Abstract from PubMed
We engineered a disulfide-stabilized influenza hemagglutinin (HA) trimer, termed HA3-SS, by introducing cysteine residues in the HA stem to covalently bridge the three protomers. HA3-SS has increased thermostability compared to wild-type HA and binding of head- and stem-targeted antibodies is preserved; only minor structural changes are found in the vicinity of the additional disulfide. This platform has been applied to H1 and H3 HAs and provides prospects for design of intact, stabilized influenza HA immunogens.
Design and Structure of an Engineered Disulfide-Stabilized Influenza Hemagglutinin Trimer.,Lee PS, Zhu X, Yu W, Wilson IA J Virol. 2015 Apr 29. pii: JVI.00808-15. PMID:25926650[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lee PS, Zhu X, Yu W, Wilson IA. Design and Structure of an Engineered Disulfide-Stabilized Influenza Hemagglutinin Trimer. J Virol. 2015 Apr 29. pii: JVI.00808-15. PMID:25926650 doi:http://dx.doi.org/10.1128/JVI.00808-15
