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Hemagglutinin





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Inmolecular biology, hemagglutinins (alternatively spelt haemagglutinin, from the Greek haima, 'blood' + Latin gluten, 'glue') are receptor-binding membrane fusion glycoproteins produced by viruses in the Paramyxoviridae and Orthomyxoviridae families.[1][2] Hemagglutinins are responsible for binding to receptors on host cells to initiate viral attachment and infection.[3]

Illustration showing influenza virus attaching to cell membrane via the surface protein hemagglutinin

Hemagglutinins recognize cell-surface glycoconjugates containing sialic acid on the surface of host red blood cells with a low affinity and use them to enter the endosome of host cells.[4] In the endosome, hemagglutinins are activated at a pH of 5–6.5 to undergo conformational changes that enable viral attachment through a fusion peptide.[5]

Virologist George K. Hirst discovered agglutination and hemagglutinins in 1941.[6] Alfred Gottschalk proved in 1957 that hemagglutinins bind a virus to a host cell by attaching to sialic acidsoncarbohydrate side chains of cell-membrane glycoproteins and glycolipids.[7]

The name "hemagglutinin" comes from the protein's ability to cause red blood cells (erythrocytes) to clump together ("agglutinate") in vitro.[8]

Types

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Structure

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Hemagglutinins are small proteins that project from the virus membrane surface as 135 Angstrom (Å) long spikes with a diameter of 30–50 Å.[14] Each spike is made up of three identical monomer subunits, making the protein a homotrimer. These monomers are formed of two glycopeptides, HA1 and HA2, and linked by two disulphide polypeptides, including membrane-distal HA1 and the smaller membrane-proximal HA2. X-ray crystallography and spectroscopy were used to identify that the majority of the protein structures is made of α-helical proteins.[15] In addition to the homotrimeric core structure, hemagglutinins have four subdomains: the membrane-distal receptor binding R subdomain, the vestigial domain E, that functions as a receptor-destroying esterase, the fusion domain F, and the membrane anchor subdomain M. The membrane anchor subdomain forms elastic protein chains linking the hemagglutinin to the ectodomain.[16]

Uses in serology

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A schematic diagram of the experimental setup to detect hemagglutination for blood typing.

See also

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References

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  1. ^ Couch, Robert B. (1996), Baron, Samuel (ed.), "Orthomyxoviruses", Medical Microbiology (4th ed.), Galveston (TX): University of Texas Medical Branch at Galveston, ISBN 978-0-9631172-1-2, PMID 21413353, retrieved 30 January 2024
  • ^ "Paramyxoviridae - an overview | ScienceDirect Topics". www.sciencedirect.com. Retrieved 30 January 2024.
  • ^ Nobusawa, E. (October 1997). "[Structure and function of the hemagglutinin of influenza viruses]". Nihon Rinsho. Japanese Journal of Clinical Medicine. 55 (10): 2562–2569. ISSN 0047-1852. PMID 9360372.
  • ^ Bangaru, Sandhya; Lang, Shanshan; Schotsaert, Michael; Vanderven, Hillary A.; Zhu, Xueyong; Kose, Nurgun; Bombardi, Robin; Finn, Jessica A.; Kent, Stephen J.; Gilchuk, Pavlo; Gilchuk, Iuliia (2019). "A Site of Vulnerability on the Influenza Virus Hemagglutinin Head Domain Trimer Interface". Cell. 177 (5): 1136–1152.e18. doi:10.1016/j.cell.2019.04.011. PMC 6629437. PMID 31100268.
  • ^ Medeiros, R.; Escriou, N.; Naffakh, N.; Manuguerra, J. C.; van der Werf, S. (10 October 2001). "Hemagglutinin residues of recent human A(H3N2) influenza viruses that contribute to the inability to agglutinate chicken erythrocytes". Virology. 289 (1): 74–85. doi:10.1006/viro.2001.1121. ISSN 0042-6822. PMID 11601919.
  • ^ Kolata, Gina (26 January 1994). "George Keble Hirst, 84, Is Dead; A Pioneer in Molecular Virology". The New York Times. ISSN 0362-4331. Retrieved 14 May 2024.
  • ^ Henry, Ronnie; Murphy, Frederick A. (October 2018). "Etymologia: Hemagglutinin and Neuraminidase". Emerging Infectious Diseases. 24 (10): 1849. doi:10.3201/eid2410.ET2410. PMC 6154157.
  • ^ Nelson DL, Cox MM (2005). Lehninger's Principles of Biochemistry (4th ed.). New York: WH Freeman.
  • ^ CDC (2 November 2021). "Types of Influenza Viruses". Centers for Disease Control and Prevention. Retrieved 18 October 2022.
  • ^ Hashiguchi, Takao; Maenaka, Katsumi; Yanagi, Yusuke (16 December 2011). "Measles Virus Hemagglutinin: Structural Insights into Cell Entry and Measles Vaccine". Frontiers in Microbiology. 2: 247. doi:10.3389/fmicb.2011.00247. ISSN 1664-302X. PMC 3267179. PMID 22319511.
  • ^ Pan CH, Jimenez GS, Nair N (21 August 2014) [August, 2008]. "Use of Vaxfectin Adjuvant with DNA Vaccine Encoding the Measles Virus Hemagglutinin and Fusion Proteins Protects Juvenile and Infant Rhesus Macaques against Measles Virus". Clinical and Vaccine Immunology. 15 (8): 1214–1221. doi:10.1128/CVI.00120-08. PMC 2519314. PMID 18524884.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  • ^ Tappert, Mary M.; Porterfield, J. Zachary; Mehta-D'Souza, Padmaja; Gulati, Shelly; Air, Gillian M. (August 2013). "Quantitative Comparison of Human Parainfluenza Virus Hemagglutinin-Neuraminidase Receptor Binding and Receptor Cleavage". Journal of Virology. 87 (16): 8962–8970. doi:10.1128/JVI.00739-13. ISSN 0022-538X. PMC 3754076. PMID 23740997.
  • ^ Kubota, Marie; Hashiguchi, Takao (2020). "Large-Scale Expression and Purification of Mumps Virus Hemagglutinin-Neuraminidase for Structural Analyses and Glycan-Binding Assays". Lectin Purification and Analysis. Methods in Molecular Biology. Vol. 2132. pp. 641–652. doi:10.1007/978-1-0716-0430-4_55. ISBN 978-1-0716-0429-8. ISSN 1940-6029. PMID 32306363. S2CID 216030421.
  • ^ Gamblin, Steven J.; Vachieri, Sébastien G.; Xiong, Xiaoli; Zhang, Jie; Martin, Stephen R.; Skehel, John J. (1 October 2021). "Hemagglutinin Structure and Activities". Cold Spring Harbor Perspectives in Medicine. 11 (10): a038638. doi:10.1101/cshperspect.a038638. ISSN 2157-1422. PMC 8485738. PMID 32513673.
  • ^ Gamblin, Steven J.; Vachieri, Sébastien G.; Xiong, Xiaoli; Zhang, Jie; Martin, Stephen R.; Skehel, John J. (1 October 2021). "Hemagglutinin Structure and Activities". Cold Spring Harbor Perspectives in Medicine. 11 (10): a038638. doi:10.1101/cshperspect.a038638. ISSN 2157-1422. PMC 8485738. PMID 32513673.
  • ^ Donald J. Benton, Andrea Nans, Lesley J. Calder, Jack Turner, Ursula Neu, Yi Pu Lin, Esther Ketelaars, Nicole L. Kallewaard, Davide Corti, Antonio Lanzavecchia, Steven J. Gamblin, Peter B. Rosenthal, John J. Skehel (2 October 2018) [Sep 17, 2018]. "Hemagglutinin membrane anchor". Proceedings of the National Academy of Sciences of the United States of America. 115 (40): 10112–10117. doi:10.1073/pnas.1810927115. PMC 6176637. PMID 30224494.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  • ^ Payne, Susan (2017). "Methods to Study Viruses". Viruses. pp. 37–52. doi:10.1016/B978-0-12-803109-4.00004-0. ISBN 978-0-12-803109-4. S2CID 89981392.
  • ^ Ashiba, Hiroki; Fujimaki, Makoto; Awazu, Koichi; Fu, Mengying; Ohki, Yoshimichi; Tanaka, Torahiko; Makishima, Makoto (March 2015). "Hemagglutination detection for blood typing based on waveguide-mode sensors". Sensing and Bio-Sensing Research. 3: 59–64. doi:10.1016/j.sbsr.2014.12.003.
  • ^ Theis, Samuel R.; Hashmi, Muhammad F. (2022), "Coombs Test", StatPearls, Treasure Island (FL): StatPearls Publishing, PMID 31613487, retrieved 16 December 2022
  • ^ Focosi, Daniele; Franchini, Massimo; Maggi, Fabrizio (8 March 2022). "Modified Hemagglutination Tests for COVID-19 Serology in Resource-Poor Settings: Ready for Prime-Time?". Vaccines. 10 (3): 406. doi:10.3390/vaccines10030406. ISSN 2076-393X. PMC 8953758. PMID 35335038.
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    Last edited on 25 June 2024, at 20:06  





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    This page was last edited on 25 June 2024, at 20:06 (UTC).

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