Influenza Hemagglutinin (HA) Peptide

HA tag,Complexes containing plasmid DNA, transferrin-polylysine conjugates, and polylysine-conjugated peptides derived from the N-terminal sequence of the influenza virus hemagglutinin subunit HA-2 have been used for the transfer of luciferase or -galactosidase marker genes to K562 cells, HeLa cells, and BNL CL.2 hepatocytes. The presence of these influenza peptide conjugates in the DNA complexes renders the complexes active in membrane disruption in a liposome leakage assay and results in a substantial augmentation of the transferrin-polylysine-mediated gene transfer.

Fusogenic peptides derived from the N-terminal sequence of the influenza virus hemagglutinin subunit HA-2 is part of the DNA complexes and the resulting augmentation of gene transfer to cultured cells¹.

In the influenza virus, the hemagglutinin (HA) protein mediates both binding of the virus to the cell surface and the subsequent fusion of viral and cellular membranes. HA is composed of a receptor-binding subunit, denoted HA1, and a fusogenic subunit, denoted HA2. The native HA1yHA2 complex, as found on the surface of the native virus, is fusioninactive. For influenza virus, membrane fusion is regulated by the conformational state of the hemagglutinin (HA) protein, which switches from a native (nonfusogenic) structure to a fusion-active (fusogenic) conformation when exposed to the acidic environment of the cellular endosome. The native structure of HA is trapped in a metastable state and that the fusogenic conformation is released by destabilization of native structure².

References:
1. E. WAGNER, C. PLANK et al, Influenza virus hemagglutinin HA-2 N-terminal fusogenic peptides augment gene transfer by transferrin-polylysine-DNA complexes: Toward a synthetic virus-like gene-transfer vehicle. Proc. Nati. Acad. Sci. USA Vol. 89, pp. 7934-7938, September 1992
2. C. M. CARR, C. CHAUDHRY, P. S. KIM et al. Influenza hemagglutinin is spring-loaded by a metastable native conformation. Proc. Natl. Acad. Sci. USA Vol. 94, pp. 14306–14313

A major T cell determinant from the influenza virus hemagglutinin (HA) can be a cryptic self peptide in HA transgenic mice.[Pubmed:9040007]

Int Immunol. 1997 Feb;9(2):249-61.

Transgenic (Tg) mice expressing the influenza virus PR8 hemagglutinin (PR8 HA) were infected with PR8 virus and analyzed for their ability to generate T cell responses to individual MHC class II-restricted T cell determinants from the HA. HAmemb and HAtrunc mice each express HA transgene mRNA in many tissues (including the thymus), but differ in the form and amount of the HA that is expressed: HAmemb mice express the entire viral HA as a membrane-bound neo-self antigen, whereas HAtrunc mice express lower levels of a truncated HA polypeptide. HAmemb mice were found to mediate efficient negative selection of autoreactive T cells directed to the major I-Ed-restricted and I-Ad-restricted determinants from the HA (designated S1 and S2 respectively). S1-specific T cell responses were similarly undetectable in PR8-infected HAtrunc mice. However, S2-specific T cells were only partially eliminated in HAtrunc mice; indeed, even though their frequency was reduced relative to non-Tg mice, S2-specific T cells still constituted a sizable population in PR8-infected HAtrunc mice. Moreover, the S2-specific T cells from HAtrunc and non-Tg mice appeared to be equally sensitive to stimulation with S2 peptide, and in each case utilized highly diverse T cell receptors to recognize S2-I-Ad. The findings demonstrate that an individual class II-restricted T cell determinant can be recognized as a cryptic self peptide during T cell repertoire formation and as an immunodominant peptide in the context of an anti-viral T cell response, providing a basis for the induction of autoreactive T cells by viruses containing homologs of self antigens.

HA Peptide (HA tag) is a nine amino acids peptide derived from the human influenza hemagglutinin (HA). It is extensively used to isolate, purify, detect, and track the protein of interest in cell biology and biochemistry.

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