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Gene Review

HMHA1  -  histocompatibility (minor) HA-1

Homo sapiens

Synonyms: ARHGAP45, HA-1, HLA-HA1, KIAA0223, Minor histocompatibility protein HA-1
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Disease relevance of HMHA1


High impact information on HMHA1

  • Cytotoxic T lymphocytes (CTLs) specific for mHags of the recipients can be isolated from the blood of recipients with severe GvHD (ref. 3). A retrospective study demonstrated an association between mismatch for mHags HA-1, -2, -4 and -5 and the occurrence of GvHD in adult recipients of bone marrow from HLA genotypically identical donors [5].
  • The minor histocompatibility antigen HA-1: a diallelic gene with a single amino acid polymorphism [6].
  • Family analysis with HA-1 allele-specific polymerase chain reaction showed an exact correlation between this allelic polymorphism and the HA-1 phenotype [6].
  • The regions of antigenic variation in influenza hemagglutinin (HA) are located on surface-accessible regions in the three-dimensional structure of the HA1 monomer [7].
  • A conserved region of the hemagglutinin molecule around amino acid position 115 in the heavy chain (HA1) was implicated as being important in this recognition by the lack of stimulatory activity associated with a glutamic acid to lysine substitution at position 115 in the laboratory mutant RV6, derived from wild-type PR8 [8].

Chemical compound and disease context of HMHA1

  • At calcium-specific ionophore A23187 concentrations of approximately 0.25 microM [which still allow assembly and release of fowl plague virus (FPV) particles] post-translational proteolytic cleavage of the viral hemagglutinin precursor HA into the fragments HA1 and HA2 is inhibited [9].
  • The influenza virus hemagglutinin polypeptides, HA1 and HA2, have been purified by gel filtration in the presence of sodium dodecyl sulfate from a vaccine preparation of the recombinant strain Heq1N2 [10].
  • Low-molecular-weight inhibitors of serine proteases, aprotinin and leupeptin, when added to influenza virus-infected HAEC suppressed HA0 cleavage and reduced the amount of cleaved HA1/HA2 both in cells and in progeny virions and thus diminished the infectivity of the virus [11].
  • The haemagglutinin from the Hong Kong influenza virus A/Memphis/102/72 contains seven oligosaccharide units attached to asparagine residues 8, 22, 38, 81, 165 and 285 in the heavy chain (HA1) and to residue 154 in the light chain (HA2) [12].
  • Furthermore, extracellular reaction of GSH with cisplatin prior to treating HA1 cells reduced the toxicity of the compound, indicating that this reaction is capable of participating in the detoxification of cisplatin [13].

Biological context of HMHA1


Anatomical context of HMHA1


Associations of HMHA1 with chemical compounds

  • Vir-2 cells recognized the reduced and alkylated purified HA1 of PR8 virus, and this reactivity was retained after cleavage at methionine and tryptophan residues [8].
  • Our results show that the only difference in glycosylation between the HA1s of the virulent and avirulent strains is the lack of an asparagine-linked carbohydrate on the virulent HA1 polypeptide at residue 11 [16].
  • Their HA1 amino acid sequences differ at 10 positions, one of which (N154) introduces a potential glycosylation site in A/Vietnam/1203/04 (H5N1) [17].
  • These include a hydrophobic signal peptide, hydrophobic NH2 and COOH termini of the HA2 subunit, and a HA1/HA2 cleavage site involving an arginine residue [18].
  • (1) as the intact hemagglutinin after disruption of the virus in sodium dodecyl sulfate, giving 2 subunits of 58,000 daltons (HA1) and 26,000 daltons (HA2), and (2) after treatment of the virus with bromelain, giving 2 subunits of 58,000 daltons (BHA1) and 21,000 daltons (BHA2) [19].

Physical interactions of HMHA1


Other interactions of HMHA1

  • In contrast, the frequencies of all ABCA7 allelic variants and additional HA-1 polymorphisms were similar in patients and controls [2].
  • Since maternal cells traffic into the fetus during pregnancy, we questioned whether cord blood has the potential to generate cytotoxic T cells specific for the hematopoietic minor histocompatibility (H) antigen HA-1 that would support the graft-versus-leukemia effect [15].

Analytical, diagnostic and therapeutic context of HMHA1


  1. Expression of minor histocompatibility antigen, HA-1, in solid tumor cells. Fujii, N., Hiraki, A., Ikeda, K., Ohmura, Y., Nozaki, I., Shinagawa, K., Ishimaru, F., Kiura, K., Shimizu, N., Tanimoto, M., Harada, M. Transplantation (2002) [Pubmed]
  2. Homozygosity for the 168His variant of the minor histocompatibility antigen HA-1 is associated with reduced risk of primary Sjögren's syndrome. Harangi, M., Kaminski, W.E., Fleck, M., Orsó, E., Zeher, M., Kiss, E., Szekanecz, Z., Zilahi, E., Marienhagen, J., Aslanidis, C., Paragh, G., Bolstad, A.I., Jonsson, R., Schmitz, G. Eur. J. Immunol. (2005) [Pubmed]
  3. Quantification of the HA-1 gene product at the RNA level; relevance for immunotherapy of hematological malignancies. Wilke, M., Dolstra, H., Maas, F., Pool, J., Brouwer, R., Falkenburg, J.H., Rebello, A., Lamers, F., Schuuring, E., Kluin, P., Brasseur, F., Goulmy, E. Hematol. J. (2003) [Pubmed]
  4. Immunogenic structure of the influenza virus hemagglutinin. Green, N., Alexander, H., Olson, A., Alexander, S., Shinnick, T.M., Sutcliffe, J.G., Lerner, R.A. Cell (1982) [Pubmed]
  5. Tetrameric HLA class I-minor histocompatibility antigen peptide complexes demonstrate minor histocompatibility antigen-specific cytotoxic T lymphocytes in patients with graft-versus-host disease. Mutis, T., Gillespie, G., Schrama, E., Falkenburg, J.H., Moss, P., Goulmy, E. Nat. Med. (1999) [Pubmed]
  6. The minor histocompatibility antigen HA-1: a diallelic gene with a single amino acid polymorphism. den Haan, J.M., Meadows, L.M., Wang, W., Pool, J., Blokland, E., Bishop, T.L., Reinhardus, C., Shabanowitz, J., Offringa, R., Hunt, D.F., Engelhard, V.H., Goulmy, E. Science (1998) [Pubmed]
  7. Modulation of immunodominant sites in influenza hemagglutinin compromise antigenic variation and select receptor-binding variant viruses. Temoltzin-Palacios, F., Thomas, D.B. J. Exp. Med. (1994) [Pubmed]
  8. Influenza virus site recognized by a murine helper T cell specific for H1 strains. Localization to a nine amino acid sequence in the hemagglutinin molecule. Hackett, C.J., Dietzschold, B., Gerhard, W., Ghrist, B., Knorr, R., Gillessen, D., Melchers, F. J. Exp. Med. (1983) [Pubmed]
  9. Inhibition of proteolytic cleavage of the hemagglutinin of influenza virus by the calcium-specific ionophore A23187. Klenk, H.D., Garten, W., Rott, R. EMBO J. (1984) [Pubmed]
  10. Chromatographic isolation of the hemagglutinin polypeptides from influenza virus vaccine and determination of their amino-terminal sequences. Bucher, D.J., Li, S.S., Kehoe, J.M., Kilbourne, E.D. Proc. Natl. Acad. Sci. U.S.A. (1976) [Pubmed]
  11. Cleavage of influenza a virus hemagglutinin in human respiratory epithelium is cell associated and sensitive to exogenous antiproteases. Zhirnov, O.P., Ikizler, M.R., Wright, P.F. J. Virol. (2002) [Pubmed]
  12. Carbohydrate composition of the oligosaccharide units of the haemagglutinin from the Hong Kong influenza virus A/Memphis/102/72. Ward, C.W., Gleeson, P.A., Dopheide, T.A. Biochem. J. (1980) [Pubmed]
  13. Cellular resistance to oxidative stress is accompanied by resistance to cisplatin: the significance of increased catalase activity and total glutathione in hydrogen peroxide-resistant fibroblasts. Spitz, D.R., Phillips, J.W., Adams, D.T., Sherman, C.M., Deen, D.F., Li, G.C. J. Cell. Physiol. (1993) [Pubmed]
  14. Generation of minor histocompatibility antigen HA-1-specific cytotoxic T cells restricted by nonself HLA molecules: a potential strategy to treat relapsed leukemia after HLA-mismatched stem cell transplantation. Mutis, T., Blokland, E., Kester, M., Schrama, E., Goulmy, E. Blood (2002) [Pubmed]
  15. Cord blood comprises antigen-experienced T cells specific for maternal minor histocompatibility antigen HA-1. Mommaas, B., Stegehuis-Kamp, J.A., van Halteren, A.G., Kester, M., Enczmann, J., Wernet, P., Kögler, G., Mutis, T., Brand, A., Goulmy, E. Blood (2005) [Pubmed]
  16. Glycosylation affects cleavage of an H5N2 influenza virus hemagglutinin and regulates virulence. Deshpande, K.L., Fried, V.A., Ando, M., Webster, R.G. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  17. Role of specific hemagglutinin amino acids in the immunogenicity and protection of H5N1 influenza virus vaccines. Hoffmann, E., Lipatov, A.S., Webby, R.J., Govorkova, E.A., Webster, R.G. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  18. Evolution of influenza A and B viruses: conservation of structural features in the hemagglutinin genes. Krystal, M., Elliott, R.M., Benz, E.W., Young, J.F., Palese, P. Proc. Natl. Acad. Sci. U.S.A. (1982) [Pubmed]
  19. Studies on the primary structure of the influenza virus hemagglutinin. Skehel, J.J., Waterfield, M.D. Proc. Natl. Acad. Sci. U.S.A. (1975) [Pubmed]
  20. Genomic identification of the minor histocompatibility antigen HA-1 locus by allele-specific PCR. Wilke, M., Pool, J., den Haan, J.M., Goulmy, E. Tissue Antigens (1998) [Pubmed]
  21. Genomic typing of minor histocompatibility antigen HA-1 by reference strand mediated conformation analysis (RSCA). Aróstegui, J.I., Gallardo, D., Rodríguez-Luaces, M., Querol, S., Madrigal, J.A., García-López, J., Grañena, A. Tissue Antigens (2000) [Pubmed]
  22. HLA class I-minor histocompatibility antigen tetramers select cytotoxic T cells with high avidity to the natural ligand. Gillespie, G., Mutis, T., Schrama, E., Kamp, J., Esendam, B., Falkenburg, J.F., Goulmy, E., Moss, P. Hematol. J. (2000) [Pubmed]
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