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J Bacteriol. Feb 1994; 176(4): 941–947.
PMCID: PMC205142

Adsorption of bacteriophage lambda on the LamB protein of Escherichia coli K-12: point mutations in gene J of lambda responsible for extended host range.


LamB is the cell surface receptor for bacteriophage lambda. LamB missense mutations yielding resistance to lambda group in two classes. Class I mutants block the growth of lambda with the wild-type host range (lambda h+) but support the growth of one-step host range mutants (lambda h). Class II mutants block lambda h but support the growth of two-step host range mutant (lambda hh*) phages. To identify amino acid residues in the J protein (the tail fiber of phage lambda) responsible for the extended host range phenotype of mutants of phage (lambda h+), we selected a series of one-step (lambda h) and two-step (lambda hh*) host range mutants and analyzed their corresponding J genes. Three different class I LamB missense mutants (mutations at sites 247, 245, and 148) were used to select 11 independent, new, one-step host range mutants (lambda h phages). DNA sequence analysis revealed a single-amino-acid change in each case. The 11 alterations affected only three residues in the distal part of J, corresponding to a Val-->Ala change at site 1077 in five cases, a Thr-->Met change at site 1040 in three cases, and a Leu-->Pro change at site 1127 in three cases. Recombination experiments confirmed that in the cases tested, the mutations identified were indeed responsible for the extended host range phenotype. The class II LamB mutant (Gly-->Asp at site 151) was used to select two-step extended host range mutants (lambda hh* phages) from three new lambda h phages, corresponding to different amino acid modifications in the J protein (at sites 1040, 1077, and 1127). The new lambda hh* phages analyzed corresponded to either double or triple point mutations located at the distal end of the J protein. In all, seven residues involved in the extended host range properties of lambda mutants were identified in the distal part of the J protein, suggesting that the last C-terminal portion of the J protein participates directly in the adsorption of the phage onto LamB. In agreement with the fact that the lambda h mutants (and the lambda hh* mutants) could grow on all of the lamB class I mutations tested, we found tha the nature of the J mutations did not depend on the LamB class I mutant used to select them. This is interpreted as meaning that the mutated residues in the J protein and in the LamB mutants are not involved in allele-specific protein-protein interactions. Rather, the LamB mutations would block a step in phage adsorption, and this block would be overcome by the mutations in the J protein.

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Selected References

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  • APPLEYARD RK, MCGREGOR JF, BAIRD KM. Mutation to extended host range and the occurrence of phenotypic mixing in the temperate coliphage lambda. Virology. 1956 Aug;2(4):565–574. [PubMed]
  • Braun-Breton C, Hofnung M. In vivo and in vitro functional alterations of the bacteriophage lambda receptor in lamB missense mutants of Escherichia coli K-12. J Bacteriol. 1981 Dec;148(3):845–852. [PMC free article] [PubMed]
  • Buchwald M, Siminovitch L. Production of serum-blocking material by mutants of the left arm of the lambda chromosome. Virology. 1969 May;38(1):1–7. [PubMed]
  • Charbit A, Clement JM, Hofnung M. Further sequence analysis of the phage lambda receptor site. Possible implications for the organization of the lamB protein in Escherichia coli K12. J Mol Biol. 1984 May 25;175(3):395–401. [PubMed]
  • Charbit A, Gehring K, Nikaido H, Ferenci T, Hofnung M. Maltose transport and starch binding in phage-resistant point mutants of maltoporin. Functional and topological implications. J Mol Biol. 1988 Jun 5;201(3):487–496. [PubMed]
  • Charbit A, Hofnung M. Isolation of different bacteriophages using the LamB protein for adsorption on Escherichia coli K-12. J Virol. 1985 Feb;53(2):667–671. [PMC free article] [PubMed]
  • Charbit A, Ronco J, Michel V, Werts C, Hofnung M. Permissive sites and topology of an outer membrane protein with a reporter epitope. J Bacteriol. 1991 Jan;173(1):262–275. [PMC free article] [PubMed]
  • Chung CT, Niemela SL, Miller RH. One-step preparation of competent Escherichia coli: transformation and storage of bacterial cells in the same solution. Proc Natl Acad Sci U S A. 1989 Apr;86(7):2172–2175. [PMC free article] [PubMed]
  • Clément JM, Hofnung M. Gene sequence of the lambda receptor, an outer membrane protein of E. coli K12. Cell. 1981 Dec;27(3 Pt 2):507–514. [PubMed]
  • Clément JM, Lepouce E, Marchal C, Hofnung M. Genetic study of a membrane protein: DNA sequence alterations due to 17 lamB point mutations affecting adsorption of phage lambda. EMBO J. 1983;2(1):77–80. [PMC free article] [PubMed]
  • Cowan SW, Schirmer T, Rummel G, Steiert M, Ghosh R, Pauptit RA, Jansonius JN, Rosenbusch JP. Crystal structures explain functional properties of two E. coli porins. Nature. 1992 Aug 27;358(6389):727–733. [PubMed]
  • Dove WF. Action of the lambda chromosome. I. Control of functions late in bacteriophage development. J Mol Biol. 1966 Aug;19(1):187–201. [PubMed]
  • Drexler K, Riede I, Montag D, Eschbach ML, Henning U. Receptor specificity of the Escherichia coli T-even type phage Ox2. Mutational alterations in host range mutants. J Mol Biol. 1989 Jun 20;207(4):797–803. [PubMed]
  • Ferenci T, Boos W. The role of the Escherichia coli lambda receptor in the transport of maltose and maltodextrins. J Supramol Struct. 1980;13(1):101–116. [PubMed]
  • Gehring K, Charbit A, Brissaud E, Hofnung M. Bacteriophage lambda receptor site on the Escherichia coli K-12 LamB protein. J Bacteriol. 1987 May;169(5):2103–2106. [PMC free article] [PubMed]
  • 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. [PubMed]
  • Hofnung M, Lepouce E, Braun-Breton C. General method for fine mapping of the Escherichia coli K-12 lamB gene: localization of missense mutations affecting bacteriophage lambda adsorption. J Bacteriol. 1981 Dec;148(3):853–860. [PMC free article] [PubMed]
  • JACOB F, WOLLMAN EL. Etude génétique d'un bactériophage tempéré d'Escherichia coli. l. Le système genétique du bactériophage. Ann Inst Pasteur (Paris) 1954 Dec;87(6):653–673. [PubMed]
  • Marchal C, Hofnung M. Negative dominance in gene lamB: random assembly of secreted subunits issued from different polysomes. EMBO J. 1983;2(1):81–86. [PMC free article] [PubMed]
  • Nakae T, Ishii JN. Molecular weights and subunit structure of LamB proteins. Ann Microbiol (Paris) 1982 Jan;133A(1):21–25. [PubMed]
  • Neuhaus JM. The receptor protein of phage lambda: purification, characterization and preliminary electrical studies in planar lipid bilayers. Ann Microbiol (Paris) 1982 Jan;133A(1):27–32. [PubMed]
  • Randall-Hazelbauer L, Schwartz M. Isolation of the bacteriophage lambda receptor from Escherichia coli. J Bacteriol. 1973 Dec;116(3):1436–1446. [PMC free article] [PubMed]
  • Roa M. Interaction of bacteriophage K10 with its receptor, the lamB protein of Escherichia coli. J Bacteriol. 1979 Nov;140(2):680–686. [PMC free article] [PubMed]
  • Roessner CA, Struck DK, Ihler GM. Morphology of complexes formed between bacteriophage lambda and structures containing the lambda receptor. J Bacteriol. 1983 Mar;153(3):1528–1534. [PMC free article] [PubMed]
  • Sanger F, Coulson AR, Hong GF, Hill DF, Petersen GB. Nucleotide sequence of bacteriophage lambda DNA. J Mol Biol. 1982 Dec 25;162(4):729–773. [PubMed]
  • Schirmer T, Cowan SW. Prediction of membrane-spanning beta-strands and its application to maltoporin. Protein Sci. 1993 Aug;2(8):1361–1363. [PMC free article] [PubMed]
  • Schwartz M. Reversible interaction between coliphage lambda and its receptor protein. J Mol Biol. 1975 Nov 25;99(1):185–201. [PubMed]
  • 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. [PMC free article] [PubMed]
  • Thirion JP, Hofnung M. On some genetic aspects of phage lambda resistance in E. coli K12. Genetics. 1972 Jun;71(2):207–216. [PMC free article] [PubMed]
  • Weiss MS, Schulz GE. Structure of porin refined at 1.8 A resolution. J Mol Biol. 1992 Sep 20;227(2):493–509. [PubMed]

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