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. 1974 Sep;14(3):503–508. doi: 10.1128/jvi.14.3.503-508.1974

Localization of Coliphage MS2 A-Protein

Linda K Curtiss 1, Robert G Krueger 2
PMCID: PMC355543  PMID: 4853028

Abstract

The purification of coliphage MS2 dinitrophenol (DNP) conjugates provided a system for localization of the single molecule of A-protein in the capsid of the MS2 phage particle. Three A-protein preparations isolated from unconjugated MS2, overconjugated DNP-MS2, and purified 78S DNP-MS2 were tested for the presence of covalently bound DNP. The binding characteristics to Dowex 1-X8 and rabbit anti-DNP bovine serum albumin (DNP-BSA) immunoglobulin G of the 78S DNP-MS2 and overconjugated DNP-MS2 A-protein preparations indicate that the A-protein is located on the surface of the phage particle where it can be covalently conjugated with hapten. Extensive enzymatic iodination of the A-protein of intact unconjugated MS2 substantiates this conclusion.

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Selected References

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

  1. Curtiss L. K., Krueger R. G. Purification and characterization of coliphage MS2 hapten conjugates. J Immunol. 1973 Jan;110(1):167–174. [PubMed] [Google Scholar]
  2. DAVIS B. J. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964 Dec 28;121:404–427. doi: 10.1111/j.1749-6632.1964.tb14213.x. [DOI] [PubMed] [Google Scholar]
  3. EISEN H. N. PREPARATION OF PURIFIED ANTI-2,4-DINITROPHENYL ANTIBODIES. Methods Med Res. 1964;10:94–102. [PubMed] [Google Scholar]
  4. Heisenberg M. Formation of defective bacteriophage particles by fr amber mutants. J Mol Biol. 1966 May;17(1):136–144. doi: 10.1016/s0022-2836(66)80100-6. [DOI] [PubMed] [Google Scholar]
  5. Hohn T., Hohn B. Structure and assembly of simple RNA bacteriophages. Adv Virus Res. 1970;16:43–98. doi: 10.1016/s0065-3527(08)60021-4. [DOI] [PubMed] [Google Scholar]
  6. Hornick C. L., Karush F. The interaction of hapten-coupled bacteriophage phi-X-174 with antihapten antibody. Isr J Med Sci. 1969 Mar-Apr;5(2):163–170. [PubMed] [Google Scholar]
  7. Kaerner H. C. Sequential steps in the in vivo assembly of the RNA bacteriophage fr. J Mol Biol. 1970 Nov 14;53(3):515–529. doi: 10.1016/0022-2836(70)90081-1. [DOI] [PubMed] [Google Scholar]
  8. Karush F. Affinity and the immune response. Ann N Y Acad Sci. 1970 Feb 13;169(1):56–64. doi: 10.1111/j.1749-6632.1970.tb55970.x. [DOI] [PubMed] [Google Scholar]
  9. King T. P., Norman P. S., Tao N. Chemical modifications of the major allergen of ragweed pollen, antigen E. Immunochemistry. 1974 Feb;11(2):83–92. doi: 10.1016/0019-2791(74)90321-8. [DOI] [PubMed] [Google Scholar]
  10. Krahn P. M., O'Callaghan R. J., Paranchych W. Stages in phage R17 infection. VI. Injection of A protein and RNA into the host cell. Virology. 1972 Mar;47(3):628–637. doi: 10.1016/0042-6822(72)90552-1. [DOI] [PubMed] [Google Scholar]
  11. Lodish H. F. Bacteriophage f2 RNA: control of translation and gene order. Nature. 1968 Oct 26;220(5165):345–350. doi: 10.1038/220345a0. [DOI] [PubMed] [Google Scholar]
  12. O'Callaghan R., Bradley R., Paranchych W. Controlled alterations in the physical and biological properties of R17 bacteriophage induced by gunaidine hydrochloride. Virology. 1973 Aug;54(2):476–494. doi: 10.1016/0042-6822(73)90158-x. [DOI] [PubMed] [Google Scholar]
  13. Osborn M., Weiner A. M., Weber K. Large scale purification of A-protein from bacterior17. Eur J Biochem. 1970 Nov;17(1):63–67. doi: 10.1111/j.1432-1033.1970.tb01134.x. [DOI] [PubMed] [Google Scholar]
  14. Phillips D. R., Morrison M. The arrangement of proteins in the human erythrocyte membrane. Biochem Biophys Res Commun. 1970 Jul 27;40(2):284–289. doi: 10.1016/0006-291x(70)91007-7. [DOI] [PubMed] [Google Scholar]
  15. Richelson E., Nathans D. Association of bacteriophage proteins and RNA in E. coli infected with MS2. Biochem Biophys Res Commun. 1967 Dec 29;29(6):842–849. doi: 10.1016/0006-291x(67)90296-3. [DOI] [PubMed] [Google Scholar]
  16. Roberts J. W., Steitz J. E. The reconstitution of infective bacteriophage R17. Proc Natl Acad Sci U S A. 1967 Oct;58(4):1416–1421. doi: 10.1073/pnas.58.4.1416. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Rohrmann G. F., Krueger R. G. Physical, biochemical, and immunological properties of coliphage MS-2 particles. J Virol. 1970 Sep;6(3):269–279. doi: 10.1128/jvi.6.3.269-279.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Rombauts W. A., Schroeder W. A., Morrison M. Bovine lactoperoxidase. Partial characterization of the further purified protein. Biochemistry. 1967 Oct;6(10):2965–2977. doi: 10.1021/bi00862a002. [DOI] [PubMed] [Google Scholar]
  19. Sefton B. M., Wickus G. G., Burge B. W. Enzymatic iodination of Sindbis virus proteins. J Virol. 1973 May;11(5):730–735. doi: 10.1128/jvi.11.5.730-735.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Stanley P., Haslam E. A. The polypeptides of influenza virus. V. Localization of polypeptides in the virion by iodination techniques. Virology. 1971 Dec;46(3):764–773. doi: 10.1016/0042-6822(71)90078-x. [DOI] [PubMed] [Google Scholar]
  21. Steitz J. A. Isolation of the A protein from bacteriphage R17. J Mol Biol. 1968 May 14;33(3):937–945. doi: 10.1016/0022-2836(68)90329-x. [DOI] [PubMed] [Google Scholar]
  22. VALENTINE R. C., STRAND M. COMPLEXES OF F-PILI AND RNA BACTERIOPHAGE. Science. 1965 Apr 23;148(3669):511–513. doi: 10.1126/science.148.3669.511. [DOI] [PubMed] [Google Scholar]
  23. Valentine R. C., Ward R., Strand M. The replication cycle of RNA bacteriophages. Adv Virus Res. 1969;15:1–59. doi: 10.1016/s0065-3527(08)60873-8. [DOI] [PubMed] [Google Scholar]
  24. Viñuela E., Algranati I. D., Ochoa S. Synthesis of virus-specific proteins in Escherichia coli infected with the RNA bacteriophage MS2. Eur J Biochem. 1967 Mar;1(1):3–11. doi: 10.1007/978-3-662-25813-2_2. [DOI] [PubMed] [Google Scholar]
  25. Witte O. N., Slobin L. I. Neutralization of haptenated bacteriophage f2 by anti-hapten antibodies: direct evidence for a critical site. J Immunol. 1972 Apr;108(4):927–936. [PubMed] [Google Scholar]

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