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Gene Review

A56R  -  temporal expression: early/late

Vaccinia virus

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Disease relevance of A56R


High impact information on A56R


Chemical compound and disease context of A56R


Biological context of A56R


Anatomical context of A56R


Associations of A56R with chemical compounds

  • Antisera to IHD-W lacking hemagglutinin-inhibiting antibodies did not precipitate the 89K glycoprotein of IHD-J [1].
  • The position of gp65 was found to correspond to the position of trimeric influenza hemagglutinin which was analyzed on a parallel sucrose gradient, suggesting that gp65 also exists as a trimer in this fraction [19].
  • Seventeen other virus strains displayed only limited growth which was primarily restricted to the initial C6/36 passage or was detected by hemagglutinin reactions without observable cell degeneration [20].

Other interactions of A56R

  • B5R is the third vaccinia gene shown to encode an EEV glycoprotein, the others being the virus hemagglutinin gene, and gene SalL4R which encodes a group of lectin-like glycoproteins of M(r) 22-24 K [21].
  • Target cells sensitized with heat-treated virus were recognized by all 11 CTL clones that were specific for internal virion proteins (nucleoprotein and basic polymerase 1), and by one of six clones specific for the major viral glycoprotein (the hemagglutinin) [22].

Analytical, diagnostic and therapeutic context of A56R


  1. Identification of the vaccinia hemagglutinin polypeptide from a cell system yielding large amounts of extracellular enveloped virus. Payne, L.G. J. Virol. (1979) [Pubmed]
  2. Sequences of the raccoon poxvirus hemagglutinin protein. Cavallaro, K.F., Esposito, J.J. Virology (1992) [Pubmed]
  3. Recombinant vaccinia virus: immunization against multiple pathogens. Perkus, M.E., Piccini, A., Lipinskas, B.R., Paoletti, E. Science (1985) [Pubmed]
  4. Surface expression of viral glycoproteins is polarized in epithelial cells infected with recombinant vaccinia viral vectors. Stephens, E.B., Compans, R.W., Earl, P., Moss, B. EMBO J. (1986) [Pubmed]
  5. Influenza virus hemagglutinin with multibasic cleavage site is activated by furin, a subtilisin-like endoprotease. Stieneke-Gröber, A., Vey, M., Angliker, H., Shaw, E., Thomas, G., Roberts, C., Klenk, H.D., Garten, W. EMBO J. (1992) [Pubmed]
  6. Analysis of the hemagglutinin glycoprotein from mutants of vaccinia virus that accumulates on the nuclear envelope. Shida, H., Matsumoto, S. Cell (1983) [Pubmed]
  7. Mouse H-2k-restricted cytotoxic T cells recognize antigenic determinants in both the HA1 and HA2 subunits of the influenza A/PR/8/34 hemagglutinin. Gould, K.G., Scotney, H., Townsend, A.R., Bastin, J., Brownlee, G.G. J. Exp. Med. (1987) [Pubmed]
  8. Amantadine selection of a mutant influenza virus containing an acid-stable hemagglutinin glycoprotein: evidence for virus-specific regulation of the pH of glycoprotein transport vesicles. Steinhauer, D.A., Wharton, S.A., Skehel, J.J., Wiley, D.C., Hay, A.J. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  9. Polarized expression of a chimeric protein in which the transmembrane and cytoplasmic domains of the influenza virus hemagglutinin have been replaced by those of the vesicular stomatitis virus G protein. McQueen, N., Nayak, D.P., Stephens, E.B., Compans, R.W. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  10. Mapping and nucleotide sequence of the vaccinia virus gene that encodes a 14-kilodalton fusion protein. Rodriguez, J.F., Esteban, M. J. Virol. (1987) [Pubmed]
  11. Role of conserved glycosylation sites in maturation and transport of influenza A virus hemagglutinin. Roberts, P.C., Garten, W., Klenk, H.D. J. Virol. (1993) [Pubmed]
  12. Studies of the membrane fusion activities of fusion peptide mutants of influenza virus hemagglutinin. Steinhauer, D.A., Wharton, S.A., Skehel, J.J., Wiley, D.C. J. Virol. (1995) [Pubmed]
  13. The hemagglutinin cleavability of a virulent avian influenza virus by subtilisin-like endoproteases is influenced by the amino acid immediately downstream of the cleavage site. Horimoto, T., Kawaoka, Y. Virology (1995) [Pubmed]
  14. Nucleotide sequence of the vaccinia virus hemagglutinin gene. Shida, H. Virology (1986) [Pubmed]
  15. Protection of cattle against rinderpest with vaccinia virus recombinants expressing the HA or F gene. Yilma, T., Hsu, D., Jones, L., Owens, S., Grubman, M., Mebus, C., Yamanaka, M., Dale, B. Science (1988) [Pubmed]
  16. Infection with vaccinia favors the selection of hybridomas synthesizing autoantibodies against intermediate filaments, one of them cross-reacting with the virus hemagglutinin. Dales, S., Fujinami, R.S., Oldstone, M.B. J. Immunol. (1983) [Pubmed]
  17. Deletion of the vaccinia virus B5R gene encoding a 42-kilodalton membrane glycoprotein inhibits extracellular virus envelope formation and dissemination. Wolffe, E.J., Isaacs, S.N., Moss, B. J. Virol. (1993) [Pubmed]
  18. The export of major histocompatibility complex class I molecules from the endoplasmic reticulum of rat brown adipose cells is acutely stimulated by insulin. Malide, D., Yewdell, J.W., Bennink, J.R., Cushman, S.W. Mol. Biol. Cell (2001) [Pubmed]
  19. The spleen focus-forming virus envelope glycoprotein is defective in oligomerization. Kilpatrick, D.R., Srinivas, R.V., Compans, R.W. J. Biol. Chem. (1989) [Pubmed]
  20. Susceptibility of Aedes albopictus C6/36 cells to viral infection. White, L.A. J. Clin. Microbiol. (1987) [Pubmed]
  21. A constitutively expressed vaccinia gene encodes a 42-kDa glycoprotein related to complement control factors that forms part of the extracellular virus envelope. Engelstad, M., Howard, S.T., Smith, G.L. Virology (1992) [Pubmed]
  22. Recognition of noninfectious influenza virus by class I-restricted murine cytotoxic T lymphocytes. Hosaka, Y., Sasao, F., Yamanaka, K., Bennink, J.R., Yewdell, J.W. J. Immunol. (1988) [Pubmed]
  23. Effector CD4 cells are tolerized upon exposure to parenchymal self-antigen. Higgins, A.D., Mihalyo, M.A., Adler, A.J. J. Immunol. (2002) [Pubmed]
  24. Beta 2-microglobulin-deficient mice can be protected against influenza A infection by vaccination with vaccinia-influenza recombinants expressing hemagglutinin and neuraminidase. Epstein, S.L., Misplon, J.A., Lawson, C.M., Subbarao, E.K., Connors, M., Murphy, B.R. J. Immunol. (1993) [Pubmed]
  25. An orthopoxvirus serpinlike gene controls the ability of infected cells to fuse. Turner, P.C., Moyer, R.W. J. Virol. (1992) [Pubmed]
  26. Real-time microchip PCR for detecting single-base differences in viral and human DNA. Ibrahim, M.S., Lofts, R.S., Jahrling, P.B., Henchal, E.A., Weedn, V.W., Northrup, M.A., Belgrader, P. Anal. Chem. (1998) [Pubmed]
  27. Maturation of HIV envelope glycoprotein precursors by cellular endoproteases. Moulard, M., Decroly, E. Biochim. Biophys. Acta (2000) [Pubmed]
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