Skip to main content
PMC home page
Journal of Virology logoLink to Journal of Virology
. 1984 Jan;49(1):20–25. doi: 10.1128/jvi.49.1.20-25.1984

O antigen-dependent mutant of bacteriophage T5.

K J Heller, D Bryniok
PMCID: PMC255420  PMID: 6361278

Abstract

A T5 mutant is described which showed normal infection of Escherichia coli F but virtually no infection of cells lacking the E. coli F O antigen. This was due to very poor adsorption to the O antigen-deficient cells. Inactivation kinetics with anti-T5 serum and adsorption and desorption kinetics to receptor-deficient E. coli F cells suggested that the mutation did not affect the L-shaped tail fibers which mediate binding to the O antigen. Proof was obtained from genetic data; the structural gene for the L-shaped tail fibers mapped at a different position on the T5 chromosome than did the mutated gene. Since binding of the T5 mutant to the FhuA receptor protein was strongly inhibited by ferrichrome and since the mutation could not be crossed into phage BF23, we conclude that the mutation affects the receptor binding protein of the T5 tail.

Full text

PDF

Images in this article

21Image
on p.21
25Image
on p.25

Selected References

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

  1. Ames G. F., Nikaido K. Two-dimensional gel electrophoresis of membrane proteins. Biochemistry. 1976 Feb 10;15(3):616–623. doi: 10.1021/bi00648a026. [DOI] [PubMed] [Google Scholar]
  2. Bassford P. J., Jr, kadner R. J. Genetic analysis of components involved in vitamin B12 uptake in Escherichia coli. J Bacteriol. 1977 Dec;132(3):796–805. doi: 10.1128/jb.132.3.796-805.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Braun V., Schaller K., Wolff H. A common receptor protein for phage T5 and colicin M in the outer membrane of Escherichia coli B. Biochim Biophys Acta. 1973 Sep 27;323(1):87–97. doi: 10.1016/0005-2736(73)90433-1. [DOI] [PubMed] [Google Scholar]
  4. Braun V., Wolff H. Characterization of the receptor protein for phage T5 and colicin M in the outer membrane of E. coli B. FEBS Lett. 1973 Aug 1;34(1):77–80. doi: 10.1016/0014-5793(73)80707-0. [DOI] [PubMed] [Google Scholar]
  5. Di Masi D. R., White J. C., Schnaitman C. A., Bradbeer C. Transport of vitamin B12 in Escherichia coli: common receptor sites for vitamin B12 and the E colicins on the outer membrane of the cell envelope. J Bacteriol. 1973 Aug;115(2):506–513. doi: 10.1128/jb.115.2.506-513.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. HERTEL R., MARCHI L., MULLER K. Density mutants of phage T5. Virology. 1962 Dec;18:576–581. doi: 10.1016/0042-6822(62)90060-0. [DOI] [PubMed] [Google Scholar]
  7. Hantke K., Braun V. Functional interaction of the tonA/tonB receptor system in Escherichia coli. J Bacteriol. 1978 Jul;135(1):190–197. doi: 10.1128/jb.135.1.190-197.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Heller K., Braun V. Accelerated adsorption of bacteriophage T5 to Escherichia coli F, resulting from reversible tail fiber-lipopolysaccharide binding. J Bacteriol. 1979 Jul;139(1):32–38. doi: 10.1128/jb.139.1.32-38.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Heller K., Braun V. Polymannose O-antigens of Escherichia coli, the binding sites for the reversible adsorption of bacteriophage T5+ via the L-shaped tail fibers. J Virol. 1982 Jan;41(1):222–227. doi: 10.1128/jvi.41.1.222-227.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Hendrickson H. E., McCorquodale D. J. Genetic and physiological studies of bacteriophage t5 I. An expanded genetic map of t5. J Virol. 1971 May;7(5):612–618. doi: 10.1128/jvi.7.5.612-618.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Kadner R. J., Heller K., Coulton J. W., Braun V. Genetic control of hydroxamate-mediated iron uptake in Escherichia coli. J Bacteriol. 1980 Jul;143(1):256–264. doi: 10.1128/jb.143.1.256-264.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. LANNI Y. T. Lysis inhibition with a mutant of bacteriophage T5. Virology. 1958 Jun;5(3):481–501. doi: 10.1016/0042-6822(58)90041-2. [DOI] [PubMed] [Google Scholar]
  13. Lugtenberg B., Meijers J., Peters R., van der Hoek P., van Alphen L. Electrophoretic resolution of the "major outer membrane protein" of Escherichia coli K12 into four bands. FEBS Lett. 1975 Oct 15;58(1):254–258. doi: 10.1016/0014-5793(75)80272-9. [DOI] [PubMed] [Google Scholar]
  14. McCorquodale D. J. The T-odd bacteriophages. CRC Crit Rev Microbiol. 1975 Dec;4(2):101–159. doi: 10.3109/10408417509111574. [DOI] [PubMed] [Google Scholar]
  15. 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]
  16. Orskov I., Orskov F., Jann B., Jann K. Serology, chemistry, and genetics of O and K antigens of Escherichia coli. Bacteriol Rev. 1977 Sep;41(3):667–710. doi: 10.1128/br.41.3.667-710.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Saigo K. Isolation of high-density mutants and identification of nonessential structural proteins in bacteriophage T5; dispensability of L-shaped tail fibers and a secondary major head protein. Virology. 1978 Apr;85(2):422–433. doi: 10.1016/0042-6822(78)90449-x. [DOI] [PubMed] [Google Scholar]
  18. Schwartz M. The adsorption of coliphage lambda to its host: effect of variations in the surface density of receptor and in phage-receptor affinity. J Mol Biol. 1976 May 25;103(3):521–536. doi: 10.1016/0022-2836(76)90215-1. [DOI] [PubMed] [Google Scholar]
  19. Silhavy T. J., Szmelcman S., Boos W., Schwartz M. On the significance of the retention of ligand by protein. Proc Natl Acad Sci U S A. 1975 Jun;72(6):2120–2124. doi: 10.1073/pnas.72.6.2120. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350–4354. doi: 10.1073/pnas.76.9.4350. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Zweig M., Cummings D. J. Cleavage of head and tail proteins during bacteriophage T5 assembly: selective host involvement in the cleavage of a tail protein. J Mol Biol. 1973 Nov 5;80(3):505–518. doi: 10.1016/0022-2836(73)90418-x. [DOI] [PubMed] [Google Scholar]
  22. Zweig M., Cummings D. J. Structural proteins of bacteriophage T5. Virology. 1973 Feb;51(2):443–453. doi: 10.1016/0042-6822(73)90443-1. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Virology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES