The specificity of the influenza B virus hemagglutinin receptor binding pocket: what does it bind to?
- PMID: 23996486
- DOI: 10.1002/jmr.2293
The specificity of the influenza B virus hemagglutinin receptor binding pocket: what does it bind to?
Abstract
The influenza surface glycoprotein hemagglutinin (HA) binds to sialylglycoproteins and sialylglycolipids on the surface of host cells. These sialyl-glycans, usually linked to galactose in either α2,6 or α2,3 configurations, are the receptors for the viral HA, the binding to which promotes viral attachment, membrane fusion, and internalization of the virus. This review examines all of the available receptor binding data on the influenza B HA and provides a structure recognition perspective for the receptor binding preferences of influenza B virus HA regional and egg-adapted variants. Overall, the review serves as an up-to-date compendium of the literature binding data, and the presented discussions assist the reader in reaching a consensus understanding of the receptor specificity determinants for the influenza B HA.
Keywords: hemagglutinin; influenza B; receptor specificity.
Copyright © 2013 John Wiley & Sons, Ltd.
Similar articles
-
Molecular characterization of the receptor binding structure-activity relationships of influenza B virus hemagglutinin.Acta Virol. 2013;57(3):313-32. Acta Virol. 2013. PMID: 24020757
-
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. Cell Rep. 2013. PMID: 23434510
-
Selection of receptor-binding variants of human influenza A and B viruses in baby hamster kidney cells.Virology. 1999 Sep 15;262(1):31-8. doi: 10.1006/viro.1999.9892. Virology. 1999. PMID: 10489338
-
Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin.Annu Rev Biochem. 2000;69:531-69. doi: 10.1146/annurev.biochem.69.1.531. Annu Rev Biochem. 2000. PMID: 10966468 Review.
-
The structural variability of the influenza A hemagglutinin receptor-binding site.Brief Funct Genomics. 2018 Nov 26;17(6):415-427. doi: 10.1093/bfgp/elx042. Brief Funct Genomics. 2018. PMID: 29253080 Free PMC article. Review.
Cited by
-
Virus recognition of glycan receptors.Curr Opin Virol. 2019 Feb;34:117-129. doi: 10.1016/j.coviro.2019.01.004. Epub 2019 Mar 5. Curr Opin Virol. 2019. PMID: 30849709 Free PMC article. Review.
-
Functionality of the putative surface glycoproteins of the Wuhan spiny eel influenza virus.Nat Commun. 2021 Oct 25;12(1):6161. doi: 10.1038/s41467-021-26409-2. Nat Commun. 2021. PMID: 34697321 Free PMC article.
-
A comprehensive review of influenza B virus, its biological and clinical aspects.Front Microbiol. 2024 Sep 4;15:1467029. doi: 10.3389/fmicb.2024.1467029. eCollection 2024. Front Microbiol. 2024. PMID: 39296301 Free PMC article. Review.
-
Expedient Assembly of Multiantennary N-Glycans from Common N-Glycan Cores with Orthogonal Protection for the Profiling of Glycan-Binding Proteins.J Am Chem Soc. 2025 Apr 16;147(15):12937-12948. doi: 10.1021/jacs.5c02356. Epub 2025 Apr 7. J Am Chem Soc. 2025. PMID: 40193327 Free PMC article.
-
Influenza B Virus Receptor Specificity: Closing the Gap between Binding and Tropism.Viruses. 2024 Aug 24;16(9):1356. doi: 10.3390/v16091356. Viruses. 2024. PMID: 39339833 Free PMC article. Review.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources