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. 1987 May;61(5):1708–1711. doi: 10.1128/jvi.61.5.1708-1711.1987

Polyomavirus major capsid protein VP1 is modified by tyrosine sulfuration.

J W Ludlow, R A Consigli
PMCID: PMC254161  PMID: 3033299

Abstract

Polyomavirus was propagated in primary mouse kidney cell monolayers and 35S-sulfate labeled by maintaining the infected cells in serum-free Eagle medium supplemented with 35S-labeled sodium sulfate. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of CsCI gradient-purified 35S-sulfate-labeled virions followed by fluorography indicated that the polyomavirus-coded major capsid protein VP1 incorporated this radiolabel. Two-dimensional gel electrophoresis followed by fluorography revealed 35S-sulfate incorporation into only two of the six VP1 isoelectric species (E and F). Amino acid analysis of 35S-sulfate labeled VP1 by enzymatic hydrolysis followed by two-dimensional thin-layer electrophoresis revealed the presence of 35S-sulfate-labeled tyrosine-O-sulfate.

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Selected References

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

  1. Anders D. G., Consigli R. A. Chemical cleavage of polyomavirus major structural protein VP1: identification of cleavage products and evidence that the receptor moiety resides in the carboxy-terminal region. J Virol. 1983 Oct;48(1):197–205. doi: 10.1128/jvi.48.1.197-205.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Anders D. G., Consigli R. A. Comparison of nonphosphorylated and phosphorylated species of polyomavirus major capsid protein VP1 and identification of the major phosphorylation region. J Virol. 1983 Oct;48(1):206–217. doi: 10.1128/jvi.48.1.206-217.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Balhorn R., Jackson V., Granner D., Chalkey R. Phosphorylation of the lysine-rich histones throughout the cell cycle. Biochemistry. 1975 Jun 3;14(11):2504–2511. doi: 10.1021/bi00682a033. [DOI] [PubMed] [Google Scholar]
  4. Balhorn R., Rieke W. O., Chalkley R. Rapid electrophoretic analysis for histone phosphorylation. A reinvestigation of phosphorylation of lysine-rich histone during rat liver regeneration. Biochemistry. 1971 Oct 12;10(21):3952–3959. doi: 10.1021/bi00797a024. [DOI] [PubMed] [Google Scholar]
  5. Bolen J. B., Anders D. G., Trempy J., Consigli R. A. Differences in the subpopulations of the structural proteins of polyoma virions and capsids: biological functions of the multiple VP1 species. J Virol. 1981 Jan;37(1):80–91. doi: 10.1128/jvi.37.1.80-91.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Bolen J. B., Consigli R. A. Differential adsorption of polyoma virions and capsids to mouse kidney cells and guinea pig erythrocytes. J Virol. 1979 Nov;32(2):679–683. doi: 10.1128/jvi.32.2.679-683.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Bolen J. B., Consigli R. A. Separation of neutralizing and hemagglutination-inhibiting antibody activities and specificity of antisera to sodium dodecyl sulfate-derived polypeptides of polyoma virions. J Virol. 1980 Apr;34(1):119–129. doi: 10.1128/jvi.34.1.119-129.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Brady J. N., Winston V. D., Consigli R. A. Characterization of a DNA-protein complex and capsomere subunits derived from polyoma virus by treatment with ethyleneglycol-bis-N,N'-tetraacetic acid and dithiothreitol. J Virol. 1978 Jul;27(1):193–204. doi: 10.1128/jvi.27.1.193-204.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Brady J. N., Winston V. D., Consigli R. A. Dissociation of polyoma virus by the chelation of calcium ions found associated with purified virions. J Virol. 1977 Sep;23(3):717–724. doi: 10.1128/jvi.23.3.717-724.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Brunk C. F., Leick V. Rapid equilibrium isopycnic CsC1 gradients. Biochim Biophys Acta. 1969 Mar 18;179(1):136–144. doi: 10.1016/0005-2787(69)90129-4. [DOI] [PubMed] [Google Scholar]
  11. Chamberlain J. P. Fluorographic detection of radioactivity in polyacrylamide gels with the water-soluble fluor, sodium salicylate. Anal Biochem. 1979 Sep 15;98(1):132–135. doi: 10.1016/0003-2697(79)90716-4. [DOI] [PubMed] [Google Scholar]
  12. Frearson P. M., Crawford L. V. Polyoma virus basic proteins. J Gen Virol. 1972 Feb;14(2):141–155. doi: 10.1099/0022-1317-14-2-141. [DOI] [PubMed] [Google Scholar]
  13. Frost E., Bourgaux P. Electrophoretic analysis of the structural polypeptides of polyoma virus mutants. Virology. 1975 May;65(1):286–288. doi: 10.1016/0042-6822(75)90032-x. [DOI] [PubMed] [Google Scholar]
  14. Fukui S., Numata Y., Yamashina I. Comparison of protein sulfation in control and virus-transformed baby hamster kidney cells. J Biochem. 1984 Dec;96(6):1783–1788. doi: 10.1093/oxfordjournals.jbchem.a135011. [DOI] [PubMed] [Google Scholar]
  15. Garcea R. L., Ballmer-Hofer K., Benjamin T. L. Virion assembly defect of polyomavirus hr-t mutants: underphosphorylation of major capsid protein VP1 before viral DNA encapsidation. J Virol. 1985 May;54(2):311–316. doi: 10.1128/jvi.54.2.311-316.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Gibson W. Polyoma virus proteins: a description of the structural proteins of the virion based on polyacrylamide gel electrophoresis and peptide analysis. Virology. 1974 Dec;62(2):319–336. doi: 10.1016/0042-6822(74)90395-x. [DOI] [PubMed] [Google Scholar]
  17. Heifetz A., Prager M. D. The effect of butyrate on sulfated glycoprotein biosynthesis by human kidney tumor cells. J Biol Chem. 1981 Jul 10;256(13):6529–6532. [PubMed] [Google Scholar]
  18. Hewick R. M., Fried M., Waterfield M. D. Nonhistone virion proteins of polyoma: characterisation of the particle proteins by tryptic peptide analysis by use of ion-exchange columns. Virology. 1975 Aug;66(2):408–419. doi: 10.1016/0042-6822(75)90213-5. [DOI] [PubMed] [Google Scholar]
  19. Huttner W. B. Determination and occurrence of tyrosine O-sulfate in proteins. Methods Enzymol. 1984;107:200–223. doi: 10.1016/0076-6879(84)07013-0. [DOI] [PubMed] [Google Scholar]
  20. Huttner W. B. Sulphation of tyrosine residues-a widespread modification of proteins. Nature. 1982 Sep 16;299(5880):273–276. doi: 10.1038/299273a0. [DOI] [PubMed] [Google Scholar]
  21. Mackay R. L., Consigli R. A. Early events in polyoma virus infection: attachment, penetration, and nuclear entry. J Virol. 1976 Aug;19(2):620–636. doi: 10.1128/jvi.19.2.620-636.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. McMillen J., Center M. S., Consigli R. A. Origin of the polyoma virus-associated endonuclease. J Virol. 1975 Jan;17(1):127–131. doi: 10.1128/jvi.17.1.127-131.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Moore B. R., Free S. J. Protein modification and its biological role. Int J Biochem. 1985;17(3):283–289. doi: 10.1016/0020-711x(85)90202-2. [DOI] [PubMed] [Google Scholar]
  24. Morrissey J. H. Silver stain for proteins in polyacrylamide gels: a modified procedure with enhanced uniform sensitivity. Anal Biochem. 1981 Nov 1;117(2):307–310. doi: 10.1016/0003-2697(81)90783-1. [DOI] [PubMed] [Google Scholar]
  25. O'Farrell P. H. High resolution two-dimensional electrophoresis of proteins. J Biol Chem. 1975 May 25;250(10):4007–4021. [PMC free article] [PubMed] [Google Scholar]
  26. O'Farrell P. Z., Goodman H. M. Resolution of simian virus 40 proteins in whole cell extracts by two-dimensional electrophoresis: heterogeneity of the major capsid protein. Cell. 1976 Oct;9(2):289–298. doi: 10.1016/0092-8674(76)90119-7. [DOI] [PubMed] [Google Scholar]
  27. Pinter A., Compans R. W. Sulfated components of enveloped viruses. J Virol. 1975 Oct;16(4):859–866. doi: 10.1128/jvi.16.4.859-866.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Ponder B. A., Robbins A. K., Crawford L. V. Phophorylation of polyoma and SV40 virus proteins. J Gen Virol. 1977 Oct;37(1):75–83. doi: 10.1099/0022-1317-37-1-75. [DOI] [PubMed] [Google Scholar]
  29. Prehm P., Scheid A., Choppin P. W. The carbohydrate structure of the glycoproteins of the paramyxovirus SV5 grown in bovine kidney cells. J Biol Chem. 1979 Oct 10;254(19):9669–9677. [PubMed] [Google Scholar]
  30. Raghow R., Portner A., Hsu C. H., Clark S. B., Kingsbury D. W. Charge heterogeneity in polypeptides of negative strand RNA viruses. Virology. 1978 Oct 15;90(2):214–225. doi: 10.1016/0042-6822(78)90305-7. [DOI] [PubMed] [Google Scholar]
  31. Schaffhausen B. S., Benjamin T. L. Deficiency in histone acetylation in nontransforming host range mutants of polyoma virus. Proc Natl Acad Sci U S A. 1976 Apr;73(4):1092–1096. doi: 10.1073/pnas.73.4.1092. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Smith G. L., Consigli R. A. Transient inhibition of polyoma virus synthesis by Sendai virus (parainfluenza I). I. Demonstration and nature of the inhibition by inactivated virus. J Virol. 1972 Dec;10(6):1091–1097. doi: 10.1128/jvi.10.6.1091-1097.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Yuen L. K., Consigli R. A. Generation of capsids from unstable polyoma virions. J Virol. 1983 Sep;47(3):620–625. doi: 10.1128/jvi.47.3.620-625.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Yuen L. K., Consigli R. A. Identification and protein analysis of polyomavirus assembly intermediates from infected primary mouse embryo cells. Virology. 1985 Jul 15;144(1):127–138. doi: 10.1016/0042-6822(85)90311-3. [DOI] [PubMed] [Google Scholar]

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