H
IPR013828

Haemagglutinin, HA1 chain, alpha/beta domain superfamily

InterPro entry
Short nameHemagglutn_HA1_a/b_dom_sf
Overlapping entries
 

Description

Haemagglutinin (HA) is one of two main surface fusion glycoproteins embedded in the envelope of influenza viruses, the other being neuraminidase (NA). There are sixteen known HA subtypes (H1-H16) and nine NA subtypes (N1-N9), which together are used to classify influenza viruses (e.g. H5N1). The antigenic variations in HA and NA enable the virus to evade host antibodies made to previous influenza strains, accounting for recurrent influenza epidemics
[2]
. The HA glycoprotein is present in the viral membrane as a single polypeptide (HA0), which must be cleaved by the host's trypsin-like proteases to produce two peptides (HA1 and HA2) in order for the virus to be infectious. Once HA0 is cleaved, the newly exposed N-terminal of the HA2 peptide then acts to fuse the viral envelope to the cellular membrane of the host cell, which allows the viral negative-stranded RNA to infect the host cell. The type of host protease can influence the infectivity and pathogenicity of the virus.

The haemagglutinin glycoprotein is a trimer containing three structurally distinct regions: a globular head consisting of anti-parallel β-sheets that form a β-sandwich with a jelly-roll fold (contains the receptor binding site and the HA1/HA2 cleavage site); a triple-stranded, coiled-coil, α-helical stalk; and a globular foot composed of anti-parallel β-sheets
[1, 3]
. Each monomer consists of an intact HA0 polypeptide with the HA1 and HA2 regions linked by disulphide bonds. The N terminus of HA1 provides the central strand in the 5-stranded globular foot, while the rest of the HA1 chain makes its way to the 8-stranded globular head. HA2 provides two α helices, which form part of the triple-stranded coiled-coil that stabilises the trimer, its C terminus providing the remaining strands of the 5-stranded globular foot.

This superfamily represents a subdomain of the HA1 peptide that occurs following HA0 cleavage. This subdomain has an α/β structure.

References

1.Structure and receptor specificity of the hemagglutinin from an H5N1 influenza virus. Stevens J, Blixt O, Tumpey TM, Taubenberger JK, Paulson JC, Wilson IA. Science 312, 404-10, (2006). View articlePMID: 16543414

2.The factors of virulence of influenza a virus. Fislova T, Kostolansky F. Acta Virol. 49, 147-57, (2005). PMID: 16178512

3.Plasticity of influenza haemagglutinin fusion peptides and their interaction with lipid bilayers. Vaccaro L, Cross KJ, Kleinjung J, Straus SK, Thomas DJ, Wharton SA, Skehel JJ, Fraternali F. Biophys. J. 88, 25-36, (2005). View articlePMID: 15475582

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