Specificity of Diffusion Channels Produced by Lambda Phage Receptor Protein of Escherichia Coli

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1980 Jan 1

PMID 6444720

Citations 93

Authors

M Luckey

H Nikaido

Affiliations

Soon will be listed here.

Abstract

The lamB protein, the receptor for phage lambda, was purified from the outer membrane of Escherichia coli K-12 by extraction with Triton X-100 and EDTA, chromatography on DEAE-Sephacel in Triton X-100, exchange of Triton for cholate by gel filtration, and chromatography on Sephacryl S-200 in cholate, NaCl, and EDTA. The purified protein appeared to exist as several oligomeric species. In an equilibrium retention assay with reconstituted vesicles containing phospholipids and lipopolysaccharide, the lamB protein conferred permeability for disaccharides. In a liposome swelling assay designed to measure rates of diffusion, the lamB protein conferred permeability to phospholipid liposomes for a variety of substrates. The rates obtained indicate the permeation facilitated by the lamB protein is specific, discriminating among substrates by both size and configuration. For example, maltose diffused into liposomes 40 times faster than sucrose, about 8 times faster than cellobiose, and about 12 times faster than maltoheptaose. The results suggest that the lamB protein forms a transmembrane channel containing a site (or sites) that loosely interacts with the solutes.

Citing Articles

Interplay between porin deficiency, fitness, and virulence in carbapenem-non-susceptible Pseudomonas aeruginosa and Enterobacteriaceae.

Mammeri H, Sereme Y, Toumi E, Faury H, Skurnik D PLoS Pathog. 2025; 21(2):e1012902.

PMID: 39919103 PMC: 11805372. DOI: 10.1371/journal.ppat.1012902.

Fosfomycin Uptake in Is Mediated by the Outer-Membrane Porins OmpF, OmpC, and LamB.

Bianchi M, Winterhalter M, Harbig T, Horompoli D, Ghai I, Nieselt K ACS Infect Dis. 2023; 10(1):127-137.

PMID: 38104323 PMC: 10789261. DOI: 10.1021/acsinfecdis.3c00367.

The Whole Is Bigger than the Sum of Its Parts: Drug Transport in the Context of Two Membranes with Active Efflux.

Rybenkov V, Zgurskaya H, Ganguly C, Leus I, Zhang Z, Moniruzzaman M Chem Rev. 2021; 121(9):5597-5631.

PMID: 33596653 PMC: 8369882. DOI: 10.1021/acs.chemrev.0c01137.

Engineering of a new strain efficiently metabolizing cellobiose with promising perspectives for plant biomass-based application design.

Borne R, Vita N, Franche N, Tardif C, Perret S, Fierobe H Metab Eng Commun. 2021; 12:e00157.

PMID: 33457204 PMC: 7797564. DOI: 10.1016/j.mec.2020.e00157.

Conformational rearrangements in the N-domain of FepA during ferric enterobactin transport.

Majumdar A, Trinh V, Moore K, Smallwood C, Kumar A, Yang T J Biol Chem. 2020; 295(15):4974-4984.

PMID: 32098871 PMC: 7152776. DOI: 10.1074/jbc.RA119.011850.

References

de Gier J, Mandersloot J, Van Deenen L . Lipid composition and permeability of liposomes. Biochim Biophys Acta. 1968; 150(4):666-75. DOI: 10.1016/0005-2736(68)90056-4. View

LOWRY O, ROSEBROUGH N, FARR A, RANDALL R . Protein measurement with the Folin phenol reagent. J Biol Chem. 1951; 193(1):265-75. View

Kagawa Y . Reconstitution of oxidative phosphorylation. Biochim Biophys Acta. 1972; 265(3):297-338. View

Schwartz M . Isolation of the bacteriophage lambda receptor from Escherichia coli. J Bacteriol. 1973; 116(3):1436-46. PMC: 246503. DOI: 10.1128/jb.116.3.1436-1446.1973. View

Hofnung M . Divergent operons and the genetic structure of the maltose B region in Escherichia coli K12. Genetics. 1974; 76(2):169-84. PMC: 1213059. DOI: 10.1093/genetics/76.2.169. View

Smit J, Kamio Y, Nikaido H . Outer membrane of Salmonella typhimurium: chemical analysis and freeze-fracture studies with lipopolysaccharide mutants. J Bacteriol. 1975; 124(2):942-58. PMC: 235985. DOI: 10.1128/jb.124.2.942-958.1975. View

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; 58(1):254-8. DOI: 10.1016/0014-5793(75)80272-9. View

Nakae T . Outer membrane of Salmonella. Isolation of protein complex that produces transmembrane channels. J Biol Chem. 1976; 251(7):2176-8. View

Chong C, Colbow K . Light scattering and turbidity measurements on lipid vesicles. Biochim Biophys Acta. 1976; 436(2):260-82. DOI: 10.1016/0005-2736(76)90192-9. View

10.

Szmelcman S, Schwartz M, Silhavy T, 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; 65(1):13-9. DOI: 10.1111/j.1432-1033.1976.tb10383.x. View

11.

Decad G, Nikaido H . Outer membrane of gram-negative bacteria. XII. Molecular-sieving function of cell wall. J Bacteriol. 1976; 128(1):325-36. PMC: 232859. DOI: 10.1128/jb.128.1.325-336.1976. View

12.

Braun V . Interrelationship of the phage lambda receptor protein and maltose transport in mutants of Escherichia coli K12. Biochim Biophys Acta. 1977; 469(1):89-98. DOI: 10.1016/0005-2736(77)90328-5. View

13.

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; 78(3):1100-7. DOI: 10.1016/0006-291x(77)90534-4. View

14.

Bavoil P, Nikaido H, von Meyenburg K . Pleiotropic transport mutants of Escherichia coli lack porin, a major outer membrane protein. Mol Gen Genet. 1977; 158(1):23-33. DOI: 10.1007/BF00455116. View

15.

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; 88(1):71-4. DOI: 10.1016/0014-5793(78)80609-7. View

16.

Kagawa Y . Reconstitution of the energy transformer, gate and channel subunit reassembly, crystalline ATPase and ATP synthesis. Biochim Biophys Acta. 1978; 505(1):45-93. DOI: 10.1016/0304-4173(78)90008-3. View

17.

Hancock R, Nikaido H . Outer membranes of gram-negative bacteria. XIX. Isolation from Pseudomonas aeruginosa PAO1 and use in reconstitution and definition of the permeability barrier. J Bacteriol. 1978; 136(1):381-90. PMC: 218670. DOI: 10.1128/jb.136.1.381-390.1978. View

18.

Sandermann Jr H, Bavoil P, Nikaido H . Phage lambda receptor protein from Escherichia coli. Solubilization and purification in an aprotic solvent. FEBS Lett. 1978; 95(1):107-10. DOI: 10.1016/0014-5793(78)80062-3. View

19.

Boos W, Dieterle R, Benz R . Receptor for bacteriophage lambda of Escherichia coli forms larger pores in black lipid membranes than the matrix protein (porin). J Bacteriol. 1979; 138(1):33-9. PMC: 218234. DOI: 10.1128/jb.138.1.33-39.1979. View

20.

Nakae T . A porin activity of purified lambda-receptor protein from Escherichia coli in reconstituted vesicle membranes. Biochem Biophys Res Commun. 1979; 88(3):774-81. DOI: 10.1016/0006-291x(79)91475-x. View