Hemagglutinin

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. 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.