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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
MeSH Review

Fowlpox

 
 
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Disease relevance of Fowlpox

  • The immunodominant, 39,000-molecular weight core protein (39K protein) of fowlpox virus (FP9 strain), equivalent to the vaccinia virus A4L gene product, contains highly charged domains at each end of the protein and multiple copies of a 12-amino-acid serine-rich repeat sequence in the middle of the protein [1].
  • We have examined the effect of coexpressing the cytokine interleukin-6 or gamma interferon on immune responses to a recombinant fowlpox virus expressing influenza virus hemagglutinin [2].
  • To assess the characteristics of MGC3 protein, all 10 TGA codons in the mgc3 gene, which encode a tryptophan in the Mycoplasma species, were replaced with TGG codons, and recombinant fowlpox viruses (FPV) harboring the altered mgc3 gene were constructed [3].
  • Antitumor activity of the intratumoral injection of fowlpox vectors expressing a triad of costimulatory molecules and granulocyte/macrophage colony stimulating factor in mesothelioma [4].
  • Protection of chickens with a recombinant fowlpox virus expressing the Newcastle disease virus hemagglutinin-neuraminidase gene [5].
 

High impact information on Fowlpox

 

Chemical compound and disease context of Fowlpox

  • Two specific effects of fowlpox virus infection were an accumulation of C-4 alkylated sterol intermediates and inhibition of monounsaturated fatty acid biosynthesis [10].
  • A recombinant fowlpox virus expressing the MDV gL gene was generated to characterize this glycoprotein [11].
  • Antibiotics such as spectinomycin pentahydrate or lincomycin hydrochloride monohydrate and spectinomycin sulfate tetrahydrate were used in combination with the HVT and fowl pox vaccine and none of the antibiotics appear to have an adverse effect on the efficacy of either vaccine [12].
  • A combination of spectinomycin dihydrochloride pentahydrate and lincomycin hydrochloride monohydrate as well as spectinomycin sulfate tetrahydrate were found to be compatible with the HVT and fowl pox vaccines as demonstrated by resistance after challenge with virulent MD virus or fowl pox virus [13].
  • Structural polypeptides of two plaque-purified variant isolates of fowlpox virus differing in plaque morphology and size were examined by Coomassie blue-staining and immunoblot analysis of purified virions [14].
 

Biological context of Fowlpox

  • Nevertheless a fowlpox virus gene corresponding to the vaccinia virus thymidine kinase gene was apparently lacking within the region studied and is probably located elsewhere in the genome [15].
  • Recombinant FPV-VP2 contained only the VP2 encoding region under the control of the fowlpox early/late promoter P.E/L inserted immediately downstream of the TK gene [16].
  • Three virus constructs were designed: VV-BLV1 which contained the open reading frame for envelope glycoprotein gp51 alone, under control of VVP7.5 promoter; VV-BLV2 and VV-BLV3 contained the entire gene (gp51 + gp30) coding sequence downstream of VP7.5 and the fowlpox virus early/late promoter (PFE/L) respectively [17].
  • The two regimens were based on three priming immunizations with either an expression plasmid plus a fowlpox (FP) recombinant vector or with two FP recombinant vectors, each one expressing either the SIV(mac239) gag/pol or the HIV-1env(89.6P) genes [18].
  • This provides the basis for establishing an ELISA that discriminates between the antibody response to a recombinant fowlpox vaccine (expressing NDV HN protein) and that to live and inactivated NDV [19].
 

Anatomical context of Fowlpox

 

Gene context of Fowlpox

  • Vaccinia virus was more efficient at delivering IFN-gamma-mediated protection than was fowlpox virus, which is unable to proliferate in mammalian cells [22].
  • We expressed the chimeric protein CR3, composed by CTL epitopes rich regions from, RT, Gag and Nef and conserved Th cell epitopes from gp120, gp41 and Vpr of HIV-1 in a fowlpox virus (FWPV) vector (FPCR3), and used this vector to induce HIV-specific CTL responses in mice [23].
  • Elevated IgA responses, reaching a peak 3-4 weeks after immunization, were also observed in the lungs of mice inoculated with IL-6 expressed by another vector, fowlpox virus [24].
  • An interferon-gamma-binding protein of novel structure encoded by the fowlpox virus [6].
  • RESULTS: Reactivity against gp100 was not seen in any patient before receiving fowlpox immunization [9].

References

  1. The 131-amino-acid repeat region of the essential 39-kilodalton core protein of fowlpox virus FP9, equivalent to vaccinia virus A4L protein, is nonessential and highly immunogenic. Boulanger, D., Green, P., Smith, T., Czerny, C.P., Skinner, M.A. J. Virol. (1998) [Pubmed]
  2. Selective induction of immune responses by cytokines coexpressed in recombinant fowlpox virus. Leong, K.H., Ramsay, A.J., Boyle, D.B., Ramshaw, I.A. J. Virol. (1994) [Pubmed]
  3. Identification and expression of a Mycoplasma gallisepticum surface antigen recognized by a monoclonal antibody capable of inhibiting both growth and metabolism. Yoshida, S., Fujisawa, A., Tsuzaki, Y., Saitoh, S. Infect. Immun. (2000) [Pubmed]
  4. Antitumor activity of the intratumoral injection of fowlpox vectors expressing a triad of costimulatory molecules and granulocyte/macrophage colony stimulating factor in mesothelioma. Triozzi, P.L., Aldrich, W., Allen, K.O., Lima, J., Shaw, D.R., Strong, T.V. Int. J. Cancer (2005) [Pubmed]
  5. Protection of chickens with a recombinant fowlpox virus expressing the Newcastle disease virus hemagglutinin-neuraminidase gene. Edbauer, C., Weinberg, R., Taylor, J., Rey-Senelonge, A., Bouquet, J.F., Desmettre, P., Paoletti, E. Virology (1990) [Pubmed]
  6. An interferon-gamma-binding protein of novel structure encoded by the fowlpox virus. Puehler, F., Schwarz, H., Waidner, B., Kalinowski, J., Kaspers, B., Bereswill, S., Staeheli, P. J. Biol. Chem. (2003) [Pubmed]
  7. Evaluation of prime/boost regimens using recombinant poxvirus/tyrosinase vaccines for the treatment of patients with metastatic melanoma. Lindsey, K.R., Gritz, L., Sherry, R., Abati, A., Fetsch, P.A., Goldfeder, L.C., Gonzales, M.I., Zinnack, K.A., Rogers-Freezer, L., Haworth, L., Mavroukakis, S.A., White, D.E., Steinberg, S.M., Restifo, N.P., Panicali, D.L., Rosenberg, S.A., Topalian, S.L. Clin. Cancer Res. (2006) [Pubmed]
  8. Phase I study of immunization with dendritic cells modified with fowlpox encoding carcinoembryonic antigen and costimulatory molecules. Morse, M.A., Clay, T.M., Hobeika, A.C., Osada, T., Khan, S., Chui, S., Niedzwiecki, D., Panicali, D., Schlom, J., Lyerly, H.K. Clin. Cancer Res. (2005) [Pubmed]
  9. Recombinant fowlpox viruses encoding the anchor-modified gp100 melanoma antigen can generate antitumor immune responses in patients with metastatic melanoma. Rosenberg, S.A., Yang, J.C., Schwartzentruber, D.J., Hwu, P., Topalian, S.L., Sherry, R.M., Restifo, N.P., Wunderlich, J.R., Seipp, C.A., Rogers-Freezer, L., Morton, K.E., Mavroukakis, S.A., Gritz, L., Panicali, D.L., White, D.E. Clin. Cancer Res. (2003) [Pubmed]
  10. Effects of fowlpox virus infection on lipid metabolism in cultured chicken embryo cells. Buttke, T.M., Gafford, L.G. J. Virol. (1982) [Pubmed]
  11. Identification and characterization of a Marek's disease virus gene homologous to glycoprotein L of herpes simplex virus. Yoshida, S., Lee, L.F., Yanagida, N., Nazerian, K. Virology (1994) [Pubmed]
  12. Vaccination of chickens against Marek's disease with the turkey herpesvirus vaccine using a pneumatic vaccinator. Eidson, C.S., Kleven, S.H. Poult. Sci. (1976) [Pubmed]
  13. Efficacy of turkey herpesvirus vaccine when administered simultaneously with fowl pox vaccine. Eidson, C.S., Villegas, P., Kleven, S.H. Poult. Sci. (1975) [Pubmed]
  14. Structural proteins of two different plaque-size phenotypes of fowlpox virus. Nazerian, K., Dhawale, S., Payne, W.S. Avian Dis. (1989) [Pubmed]
  15. Similar genetic organization between a region of fowlpox virus DNA and the vaccinia virus HindIII J fragment despite divergent location of the thymidine kinase gene. Drillien, R., Spehner, D., Villeval, D., Lecocq, J.P. Virology (1987) [Pubmed]
  16. Infectious bursal disease virus structural protein VP2 expressed by a fowlpox virus recombinant confers protection against disease in chickens. Heine, H.G., Boyle, D.B. Arch. Virol. (1993) [Pubmed]
  17. Expression of bovine leukaemia virus envelope gene by recombinant vaccinia viruses. Kumar, S., Andrew, M.E., Boyle, D.B., Brandon, R.B., Lavin, M.F., Daniel, R.C. Virus Res. (1990) [Pubmed]
  18. Evaluation in rabbits of different anti-SHIV vaccine strategies based on DNA/fowlpox priming and virus-like particle boosting. Zanotto, C., Elli, V., Basavecchia, V., Brivio, A., Paganini, M., Pinna, D., Vicenzi, E., De Giuli Morghen, C., Radaelli, A. FEMS Immunol. Med. Microbiol. (2003) [Pubmed]
  19. Antibody detection-based differential ELISA for NDV-infected or vaccinated chickens versus NDV HN-subunit vaccinated chickens. Makkay, A.M., Krell, P.J., Nagy, E. Vet. Microbiol. (1999) [Pubmed]
  20. Cytotoxic T lymphocyte response in chickens immunized with a recombinant fowlpox virus expressing Marek's disease herpesvirus glycoprotein B. Omar, A.R., Schat, K.A., Lee, L.F., Hunt, H.D. Vet. Immunol. Immunopathol. (1998) [Pubmed]
  21. Improved technique for transient expression and negative strand virus rescue using fowlpox T7 recombinant virus in mammalian cells. Das, S.C., Baron, M.D., Skinner, M.A., Barrett, T. J. Virol. Methods (2000) [Pubmed]
  22. Use of recombinant viruses to deliver cytokines influencing the course of experimental bacterial infection. Cheers, C., Janas, M., Ramsay, A., Ramshaw, I. Immunol. Cell Biol. (1999) [Pubmed]
  23. The HIV-1 chimeric protein CR3 expressed by poxviral vectors induces a diverse CD8+ T cell response in mice and is antigenic for PBMCs from HIV+ patients. Vázquez-Blomquist, D., Iglesias, E., González-Horta, E.E., Duarte, C.A. Vaccine (2003) [Pubmed]
  24. Enhancement of mucosal IgA responses by interleukins 5 and 6 encoded in recombinant vaccine vectors. Ramsay, A.J., Leong, K.H., Boyle, D., Ruby, J., Ramshaw, I.A. Reprod. Fertil. Dev. (1994) [Pubmed]
 
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