Skip to main content
PMC 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 Nov;75(11):5636–5639. doi: 10.1073/pnas.75.11.5636

Protein Ia and the lamB protein can replace each other in the constitution of an active receptor for the same coliphage.

C Wandersman, M Schwartz
PMCID: PMC393022  PMID: 364487

Abstract

Protein Ia and the lamB protein are both located in the outer membrane of Escherichia coli K-12. The lamB protein is known to be the receptor for phage lambda. Datta et al. [Datta, D. B., Arden, B. & Henning, U. (1977) J. Bacteriol. 131, 821--829] recently isolated a phage called TuIa that uses protein Ia for its adsorption. While phage TuIa fails to grow on ompB mutants, which lack protein Ia, we show here that host-range mutants of TuIa can be isolated that do grow on ompB strains. These host-range mutants fail to grow on ompB lamB double mutants, but retain the ability of the parental phage to grow on ompB+ lamB strains. They are therefore apparently able to use either protein Ia or the lamB protein for their adsorption. Genetic evidence suggests that essentially the same site on the lamB protein may be interacting with phage lambda or the host-range mutants of phage TuIa.

Full text

PDF
5636

Selected References

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

  1. Arscott P. G., Goldberg E. B. Cooperative action of the T4 tail fibers and baseplate in triggering conformational change and in determining host range. Virology. 1976 Jan;69(1):15–22. doi: 10.1016/0042-6822(76)90190-2. [DOI] [PubMed] [Google Scholar]
  2. Bachmann B. J., Low K. B., Taylor A. L. Recalibrated linkage map of Escherichia coli K-12. Bacteriol Rev. 1976 Mar;40(1):116–167. doi: 10.1128/br.40.1.116-167.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bassford P. J., Jr, Diedrich D. L., Schnaitman C. L., Reeves P. Outer membrane proteins of Escherichia coli. VI. Protein alteration in bacteriophage-resistant mutants. J Bacteriol. 1977 Aug;131(2):608–622. doi: 10.1128/jb.131.2.608-622.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Bassford P. J., Jr, Schnaitman C. A., Kadner R. J. Functional stability of the bfe and tonB gene products in Escherichia coli. J Bacteriol. 1977 May;130(2):750–758. doi: 10.1128/jb.130.2.750-758.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Bavoil P., Nikaido H., von Meyenburg K. Pleiotropic transport mutants of Escherichia coli lack porin, a major outer membrane protein. Mol Gen Genet. 1977 Dec 14;158(1):23–33. doi: 10.1007/BF00455116. [DOI] [PubMed] [Google Scholar]
  6. Braun-Breton C., Hofnung M. Explanations accounting for transduction by bacteriophage lambda in maltose negative bacteriophage lambda resistant mutants of Escherichia coli K-12. Mol Gen Genet. 1978 Feb 16;159(2):143–149. doi: 10.1007/BF00270887. [DOI] [PubMed] [Google Scholar]
  7. Braun V., Krieger-Brauer H. J. Interrelationship of the phage lambda receptor protein and maltose transport in mutants of Escherichia coli K12. Biochim Biophys Acta. 1977 Aug 15;469(1):89–98. doi: 10.1016/0005-2736(77)90328-5. [DOI] [PubMed] [Google Scholar]
  8. Chai T. J., Foulds J. Escherichia coli K-12 tolF mutants: alterations in protein composition of the outer membrane. J Bacteriol. 1977 May;130(2):781–786. doi: 10.1128/jb.130.2.781-786.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Datta D. B., Arden B., Henning U. Major proteins of the Escherichia coli outer cell envelope membrane as bacteriophage receptors. J Bacteriol. 1977 Sep;131(3):821–829. doi: 10.1128/jb.131.3.821-829.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. DiRienzo J. M., Nakamura K., Inouye M. The outer membrane proteins of Gram-negative bacteria: biosynthesis, assembly, and functions. Annu Rev Biochem. 1978;47:481–532. doi: 10.1146/annurev.bi.47.070178.002405. [DOI] [PubMed] [Google Scholar]
  11. Edermann R., Hindennach I., Henning U. Major proteins of the Escherichia coli outer cell envelope membrane. Preliminary characterization of the phage lambda receptor protein. FEBS Lett. 1978 Apr 1;88(1):71–74. doi: 10.1016/0014-5793(78)80609-7. [DOI] [PubMed] [Google Scholar]
  12. Hatfield D., Hofnung M., Schwartz M. Genetic analysis of the maltose A region in Escherichia coli. J Bacteriol. 1969 May;98(2):559–567. doi: 10.1128/jb.98.2.559-567.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Hofnung M., Hatfield D., Schwartz M. malB region in Escherichia coli K-12: characterization of new mutations. J Bacteriol. 1974 Jan;117(1):40–47. doi: 10.1128/jb.117.1.40-47.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Hofnung M., Jezierska A., Braun-Breton C. lamB mutations in E. coli K12: growth of lambda host range mutants and effect of nonsense suppressors. Mol Gen Genet. 1976 May 7;145(2):207–213. doi: 10.1007/BF00269595. [DOI] [PubMed] [Google Scholar]
  15. Lindberg A. A. Bacteriophage receptors. Annu Rev Microbiol. 1973;27:205–241. doi: 10.1146/annurev.mi.27.100173.001225. [DOI] [PubMed] [Google Scholar]
  16. Nakae T. Identification of the outer membrane protein of E. coli that produces transmembrane channels in reconstituted vesicle membranes. Biochem Biophys Res Commun. 1976 Aug 9;71(3):877–884. doi: 10.1016/0006-291x(76)90913-x. [DOI] [PubMed] [Google Scholar]
  17. Randall-Hazelbauer L., Schwartz M. Isolation of the bacteriophage lambda receptor from Escherichia coli. J Bacteriol. 1973 Dec;116(3):1436–1446. doi: 10.1128/jb.116.3.1436-1446.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Rosenbusch J. P. Characterization of the major envelope protein from Escherichia coli. Regular arrangement on the peptidoglycan and unusual dodecyl sulfate binding. J Biol Chem. 1974 Dec 25;249(24):8019–8029. [PubMed] [Google Scholar]
  19. Sarma V., Reeves P. Genetic locus (ompB) affecting a major outer-membrane protein in Escherichia coli K-12. J Bacteriol. 1977 Oct;132(1):23–27. doi: 10.1128/jb.132.1.23-27.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Schmitges C. J., Henning U. The major proteins of the Escherichia coli outer cell-envelope membrane. Heterogeneity of protein I. Eur J Biochem. 1976 Mar 16;63(1):47–52. doi: 10.1111/j.1432-1033.1976.tb10205.x. [DOI] [PubMed] [Google Scholar]
  21. Schwartz M. Reversible interaction between coliphage lambda and its receptor protein. J Mol Biol. 1975 Nov 25;99(1):185–201. doi: 10.1016/s0022-2836(75)80167-7. [DOI] [PubMed] [Google Scholar]
  22. Schwartz M. Sur l'existence chez Escherichia coli K 12 d'une régulation commune à la biosynthèse des récepteurs du bactériophage et au métabolisme du maltose. Ann Inst Pasteur (Paris) 1967 Nov;113(5):685–704. [PubMed] [Google Scholar]
  23. 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]
  24. Szmelcman S., Hofnung M. Maltose transport in Escherichia coli K-12: involvement of the bacteriophage lambda receptor. J Bacteriol. 1975 Oct;124(1):112–118. doi: 10.1128/jb.124.1.112-118.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Szmelcman S., Schwartz M., Silhavy T. J., Boos W. Maltose transport in Escherichia coli K12. A comparison of transport kinetics in wild-type and lambda-resistant mutants as measured by fluorescence quenching. Eur J Biochem. 1976 May 17;65(1):13–19. doi: 10.1111/j.1432-1033.1976.tb10383.x. [DOI] [PubMed] [Google Scholar]
  26. Thirion J. P., Hofnung M. On some genetic aspects of phage lambda resistance in E. coli K12. Genetics. 1972 Jun;71(2):207–216. doi: 10.1093/genetics/71.2.207. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. von Meyenburg K., Nikaido H. Outer membrane of gram-negative bacteria. XVII. Secificity of transport process catalyzed by the lambda-receptor protein in Escherichia coli. Biochem Biophys Res Commun. 1977 Oct 10;78(3):1100–1107. doi: 10.1016/0006-291x(77)90534-4. [DOI] [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