Characterization of <i>lamB</i> protein from the outer membrane of <i>Escherichia coli</i> that forms diffusion pores selective for maltose‐maltodextrins

Ishii, Junko; Okajima, Yoshiaki; Nakae, Taiji

doi:10.1016/0014-5793(81)80605-9

Cited by 25 publications

(13 citation statements)

References 13 publications

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“…Are the amino acid changes described here located within the 1386 epitopes or do they induce conformational changes leading to an alteration of these epitopes? Biochemical and biophysical evidence indicates that the LamB protein is a rigid, highly structured molecule, firmly embedded in the membrane (Ishii et al, 1981;Neuhaus, 1982;Schwartz, 1983). Genetic data show that missense mutations affecting the various functions of the protein are both extremely rare and generally located in a few very discrete areas of the gene (Roa and Clement, 1980;Wandersman and Schwartz, 1982;Clement et al, 1983;Charbit et al, 1984).…”

Section: Discussionmentioning

confidence: 99%

“…In its native state, the LamB protein is an oligomer composed of three identical subunits (Palva and Westerman, 1979;Neuhaus, 1982) and is exposed at both faces of the membrane (reviewed in Gabay et al, 1985). Spectroscopic data indicate that its secondary structure consists predominantly of fl-pleated sheets (Ishii et al, 1981;Neuhaus, 1982). The amino acid sequence, as deduced from the nucleotide sequence of the lamB gene (Clement and Hofnung, 1981), indicated that the polypeptide is composed of 421 amino acid residues.…”

Section: Introductionmentioning

confidence: 99%

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Mutations affecting antigenic determinants of an outer membrane protein of Escherichia coli.

Desaymard¹,

Débarbouillé²,

Jolit³

et al. 1986

The EMBO Journal

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The Escherichia coli LamB protein is located in the outer membrane. It is both a component of the maltose and maltodextrin transport system, and the receptor for phages lambda and K10. It is a trimer composed of three identical polypeptide chains, each containing 421 residues. Six independent mutants have been isolated, in which the LamB protein is altered in its interaction with one or more monoclonal antibodies specific for regions of the protein that are exposed at the cell surface. Some of the mutations also altered the binding site for phage lambda. All of the mutations were clustered in the same region of the lamB gene, corresponding to residues 333‐394 in the polypeptide. This and previous results strongly suggest that a rather large segment of the LamB polypeptide, extending from residue 315 to 401, is exposed at the outer face of the outer membrane. This segment would bear the epitopes for the four available anti‐LamB monoclonal antibodies that react with the cell surface, and part of the binding site for phage lambda.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Mutations affecting antigenic determinants of an outer membrane protein of Escherichia coli.

Desaymard¹,

Débarbouillé²,

Jolit³

et al. 1986

The EMBO Journal

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show abstract

“…The protein coded by gene lamB of the maltose operon also serves as receptors for several phages, such as λ, K10 and TP1 [48,49,50]. The molecular weight of LamB is 135.6 kDa, looking like a half-open tulip, formed by 3 identical subunits, each one having a molecular weight of 45.9 kDa [51,52,53]. A major contribution to understanding the molecular basis of the λ phage interaction with LamB receptor has come from determination of the crystal structure of LamB [54].…”

Section: Structure Of the Lamb Receptor And Interaction With Bactementioning

confidence: 99%

Interaction of Bacteriophage l with Its E. coli Receptor, LamB

Chatterjee

Rothenberg

2012

Viruses

109

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The initial step of viral infection is the binding of a virus onto the host cell surface. This first viral-host interaction would determine subsequent infection steps and the fate of the entire infection process. A basic understating of the underlining mechanism of initial virus-host binding is a prerequisite for establishing the nature of viral infection. Bacteriophage λ and its host Escherichia coli serve as an excellent paradigm for this purpose. λ phages bind to specific receptors, LamB, on the host cell surface during the infection process. The interaction of bacteriophage λ with the LamB receptor has been the topic of many studies, resulting in wealth of information on the structure, biochemical properties and molecular biology of this system. Recently, imaging studies using fluorescently labeled phages and its receptor unveil the role of spatiotemporal dynamics and divulge the importance of stochasticity from hidden variables in the infection outcomes. The scope of this article is to review the present state of research on the interaction of bacteriophage λ and its E. coli receptor, LamB.

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“…[13][14][15] The maltoporin monomer, consisting of 421 amino acid residues, folds into an 18 stranded antiparallel β-barrel with short turns at the periplasmic side and large loops facing the outer side of the cell. 15 An X-ray study of maltoporin crystals soaked with maltooligosaccharides revealed the specific sugartranslocation pathway in each pore, provided by the set of aromatic amino acid residues that form the ''greasy slide'' aligned by polar residues.…”

Section: Introductionmentioning

confidence: 99%

Docking of a Single Phage Lambda to its Membrane Receptor Maltoporin as a Time-resolved Event

Gurnev

Oppenheim

Winterhalter

et al. 2006

Journal of Molecular Biology

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Characterization of lamB protein from the outer membrane of Escherichia coli that forms diffusion pores selective for maltose‐maltodextrins

Cited by 25 publications

References 13 publications

Mutations affecting antigenic determinants of an outer membrane protein of Escherichia coli.

Mutations affecting antigenic determinants of an outer membrane protein of Escherichia coli.

Interaction of Bacteriophage l with Its E. coli Receptor, LamB

Docking of a Single Phage Lambda to its Membrane Receptor Maltoporin as a Time-resolved Event

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