Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1978 Jun;75(6):2708–2712. doi: 10.1073/pnas.75.6.2708

Amino-terminal amino acid sequence of the major structural polypeptides of avian retroviruses: sequence homology between reticuloendotheliosis virus p30 and p30s of mammalian retroviruses.

E Hunter, A S Bhown, J C Bennett
PMCID: PMC392632  PMID: 208072

Abstract

The major structural polypeptides, p30 of reticuloendotheliosis virus (REV) (strain T) and p27 of avian sarcoma virus B77, have been compared with regard to amino acid composition. NH2-terminal amino acid sequence, and immunological crossreactions. The amino acid composition of the two polypeptides is distinct, and a comparison of the first 30 NH2-terminal amino acids of REV p30 with that for the first 25 of B77 p27 yields only three homologous residues. In competition radioimmunoassays the polypeptides show no crossreactivity. A comparison of the amino acid composition and NH2-terminal amino acid sequence of REV p30 with those reported for several mammalian retrovirus p30s shows remarkable similarities. Both REV and mammalian p30s contain a large number of polar residues in their amino acid composition and show approximately 40% homology in the first 30 NH2-terminal amino acids. No crossreactivity could be observed, however, in competition radioimmunoassays between Rauscher murine leukemia virus p30 and that of REV. The observations reported here suggest a close evolutionary relationship between REV and the mammalian retroviruses.

Full text

PDF
2708

Images in this article

2709Image
on p.2709

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bender W., Chien Y. H., Chattopadhyay S., Vogt P. K., Gardner M. B., Davidson N. High-molecular-weight RNAs of AKR, NZB, and wild mouse viruses and avian reticuloendotheliosis virus all have similar dimer structures. J Virol. 1978 Mar;25(3):888–896. doi: 10.1128/jvi.25.3.888-896.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bhown A. S., Habeerb A. F. Structural studies on epsilon-prototoxin of Clostridium perfringens type D. Localization of the site of tryptic scission necessary for activation to epsilon-toxin. Biochem Biophys Res Commun. 1977 Oct 10;78(3):889–896. doi: 10.1016/0006-291x(77)90506-x. [DOI] [PubMed] [Google Scholar]
  3. Bolognesi D. P., Luftig R., Shaper J. H. Localization of RNA tumor virus polypeptides. I. Isolation of further virus substructures. Virology. 1973 Dec;56(2):549–564. doi: 10.1016/0042-6822(73)90057-3. [DOI] [PubMed] [Google Scholar]
  4. Brauer A. W., Margolies M. N., Haber E. The application of 0.1 M quadrol to the microsequence of proteins and the sequence of tryptic peptides. Biochemistry. 1975 Jul;14(13):3029–3035. doi: 10.1021/bi00684a036. [DOI] [PubMed] [Google Scholar]
  5. Cullen S. E., Schwartz B. D. An improved method for isolation of H-2 and Ia alloantigens with immunoprecipitation induced by protein A-bearing staphylococci. J Immunol. 1976 Jul;117(1):136–142. [PubMed] [Google Scholar]
  6. Famulari N. G., Buchhagen D. L., Klenk H. D., Fleissner E. Presence of murine leukemia virus envelope proteins gp70 and p15(E) in a common polyprotein of infected cells. J Virol. 1976 Nov;20(2):501–508. doi: 10.1128/jvi.20.2.501-508.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Fleissner E., Tress E. Isolation of a ribonucleoprotein structure from oncornaviruses. J Virol. 1973 Dec;12(6):1612–1615. doi: 10.1128/jvi.12.6.1612-1615.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Green R. W., Bolognesi D. P. Isolation of proteins by gel filtration in 6M guanidinium chloride: application to RNA tumor viruses. Anal Biochem. 1974 Jan;57(1):108–117. doi: 10.1016/0003-2697(74)90057-8. [DOI] [PubMed] [Google Scholar]
  9. Herman A. C., Green R. W., Bolognesi D. P., Vanaman T. C. Comparative chemical properties of avian oncornavirus polypeptides. Virology. 1975 Apr;64(2):339–348. doi: 10.1016/0042-6822(75)90110-5. [DOI] [PubMed] [Google Scholar]
  10. Hunter E., Hayman M. J., Rongey R. W., Vogt P. K. An avian sarcoma virus mutant that is temperature sensitive for virion assembly. Virology. 1976 Jan;69(1):35–49. doi: 10.1016/0042-6822(76)90192-6. [DOI] [PubMed] [Google Scholar]
  11. Kang C. Y., Temin H. M. Lack of sequence homology among RNAs of avian leukosis-sarcoma viruses, reticuloendotheliosis viruses, and chicken endogenous RNA-directed DNA polymerase activity. J Virol. 1973 Dec;12(6):1314–1324. doi: 10.1128/jvi.12.6.1314-1324.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Kang C. Y., Temin H. M. Reticuloendotheliosis virus nucleic acid sequences in cellular DNA. J Virol. 1974 Nov;14(5):1179–1188. doi: 10.1128/jvi.14.5.1179-1188.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Kessler S. W. Rapid isolation of antigens from cells with a staphylococcal protein A-antibody adsorbent: parameters of the interaction of antibody-antigen complexes with protein A. J Immunol. 1975 Dec;115(6):1617–1624. [PubMed] [Google Scholar]
  14. Levy J. A. Host range of murine xenotropic virus: replication in avian cells. Nature. 1975 Jan 10;253(5487):140–142. doi: 10.1038/253140a0. [DOI] [PubMed] [Google Scholar]
  15. Maldonado R. L., Bose H. R., Jr Group-specific antigen shared by the members of the reticuloendotheliosis virus complex. J Virol. 1976 Mar;17(3):983–990. doi: 10.1128/jvi.17.3.983-990.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Moelling K., Gelderblom H., Pauli G., Friis R. A comparative study of the avian reticuloendotheliosis virus: relationship to murine leukemia virus and viruses of the avian sarcoma-leukosis complex. Virology. 1975 Jun;65(2):546–557. doi: 10.1016/0042-6822(75)90059-8. [DOI] [PubMed] [Google Scholar]
  17. Moscovici C., Moscovici M. G., Jimenez H., Lai M. M., Hayman M. J., Vogt P. K. Continuous tissue culture cell lines derived from chemically induced tumors of Japanese quail. Cell. 1977 May;11(1):95–103. doi: 10.1016/0092-8674(77)90320-8. [DOI] [PubMed] [Google Scholar]
  18. Niall H. D., Sauer R., Allen D. W. The N-terminal amino acid sequence of two avian leukosis group specific antigens. Proc Natl Acad Sci U S A. 1970 Dec;67(4):1804–1809. doi: 10.1073/pnas.67.4.1804. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Oroszlan S., Copeland T., Summers M. R., Smythers G., Gilden R. V. Amino acid sequence homology of mammalian type C RNA virus major internal proteins. J Biol Chem. 1975 Aug 25;250(16):6232–6239. [PubMed] [Google Scholar]
  20. SARMA P. S., TURNER H. C., HUEBNER R. J. AN AVIAN LEUCOSIS GROUP-SPECIFIC COMPLEMENT FIXATION REACTION. APPLICATION FOR THE DETECTION AND ASSAY OF NON-CYTOPATHOGENIC LEUCOSIS VIRUSES. Virology. 1964 Jul;23:313–321. doi: 10.1016/0042-6822(64)90253-3. [DOI] [PubMed] [Google Scholar]
  21. Stephenson J. R., Smith E. J., Crittenden L. B., Aaronson S. A. Analysis of antigenic determinants of structural polypeptides of avian type C tumor viruses. J Virol. 1975 Jul;16(1):27–33. doi: 10.1128/jvi.16.1.27-33.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Stephenson J. R., Wilsnack R. E., Aaronson S. A. Radioimmunoassay for avian C-type virus group-specific antigen: detection in normal and virus-transformed cells. J Virol. 1973 Jun;11(6):893–899. doi: 10.1128/jvi.11.6.893-899.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Summers M. R., Smythers G. W., Oroszlan S. Thin-layer chromatography of sub-nanomole amounts of phenylthiohydantoin (PTH) amino acids on polyamide sheets. Anal Biochem. 1973 Jun;53(2):624–628. doi: 10.1016/0003-2697(73)90114-0. [DOI] [PubMed] [Google Scholar]
  24. Tarr G. E., Beecher J. F., Bell M., McKean D. J. Polyquarternary amines prevent peptide loss from sequenators. Anal Biochem. 1978 Feb;84(2):622–7?0=ENG. doi: 10.1016/0003-2697(78)90086-6. [DOI] [PubMed] [Google Scholar]
  25. Theilen G. H., Zeigel R. F., Twiehaus M. J. Biological studies with RE virus (strain T) that induces reticuloendotheliosis in turkeys, chickens, and Japanese quail. J Natl Cancer Inst. 1966 Dec;37(6):731–743. [PubMed] [Google Scholar]
  26. Van Zaane D., Dekker-Michielsen J. A., Bloemers H. P. Virus-specific precursor polypeptides in cells infected with Rauscher leukemia virus: synthesis, identification, and processing. Virology. 1976 Nov;75(1):113–129. doi: 10.1016/0042-6822(76)90011-8. [DOI] [PubMed] [Google Scholar]
  27. Zeigel R. F., Theilen G. H., Twiehaus M. J. Electron microscopic observations on RE virus (strain T) that induces reticuloendotheliosis in turkeys, chickens, and Japanese quail. J Natl Cancer Inst. 1966 Dec;37(6):709–729. [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES