In molecular biology, hemagglutinins (alternatively spelled haemagglutinin, from the Greek haima, 'blood' + Latin gluten, 'glue') are receptor-binding membrane fusion glycoproteins produced by viruses in the Paramyxoviridae and Orthomyxoviridae families.
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Hemagglutinins are responsible for binding to receptors on red blood cells to initiate viral attachment and infection. The agglutination of red cells occurs when antibodies on one cell bind to those on others, causing amorphous aggregates of clumped cells.
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. 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.
Virologist George K. Hirst discovered agglutination and hemagglutinins in 1941. Alfred Gottschalk proved in 1957 that hemagglutinins bind a virus to a host cell by attaching to sialic acids on carbohydrate side chains of cell-membrane glycoproteins and glycolipids.
Hemagglutinins are small proteins that project from the virus membrane surface as 135 Angstrom (Å) long spikes with a diameter of 30-50 Å. 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. 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.
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