Maltodextrin transport through lamb

Frontiers in Bioscience

Volumn 8, Issue SUPPL., 2003, Pages

  Charbit, Alain ^a  

^a INSERM   (France)

Author keywords

Gram negative bacteria; LamB; Lambda receptor; Maltoporin; Porins; Review; Sugar transport

Indexed keywords

BACTERIAL PROTEIN; CELL SURFACE RECEPTOR; MALTODEXTRIN; MALTOSE; OLIGOSACCHARIDE; PORIN; PROTEIN LAMB; SUGAR; UNCLASSIFIED DRUG; LAMBDA PHAGE RECEPTOR; POLYSACCHARIDE; VIRUS RECEPTOR;

BACTERIOPHAGE LAMBDA; BINDING AFFINITY; BINDING SITE; ESCHERICHIA COLI; HYDROGEN BOND; HYDROPHILICITY; HYDROPHOBICITY; NONHUMAN; OUTER MEMBRANE; REVIEW; SUGAR TRANSPORT; ACTIVE TRANSPORT; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; METABOLISM; MOLECULAR GENETICS; PHYSIOLOGY; PROTEIN CONFORMATION; PROTEIN QUATERNARY STRUCTURE; PROTEIN TERTIARY STRUCTURE;

BACTERIA (MICROORGANISMS); BACTERIOPHAGE LAMBDA; ESCHERICHIA COLI; LAMB; NEGIBACTERIA;

AMINO ACID SEQUENCE; BIOLOGICAL TRANSPORT, ACTIVE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; POLYSACCHARIDES; PORINS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, VIRUS;

EID: 1542778691     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/1046     Document Type: Review

References (66)

1. Nikaido, H., & M. Vaara. Molecular basis of bacterial outer membrane permeability. FEMS Microbiol Rev 49, 1-32 (1985)
2. Nikaido, H., & M. H. J. Saier. Transport proteins in bacteria: common themes in their design. Science 258, 936-942 (1992)
3. Benz, R., A. Schmid, T. Nakae, & G. H. Vos-Scheperkeuter. Pore formation by LamB of E. coli in lipid bilayer membranes. J Bacteriol 165, 978-986 (1986)
4. Dargent, B., A. Charbit, M. Hofnung, & F. Pattus. Effect of point mutations on the in vivo pore properties of maltoporin, a protein of E. coli outer membrane. J Mol Biol 201, 497-506 (1988)
5. Maier, C., E. Bremer, A. Schmid, & R. Benz. Pore-forming activity of the Tsx protein from the outer membrane of Escherichia coli. Demonstration of a nucleoside-specific binding site. J Biol Chem 263, 2493-2499 (1988)
6. Benz, R., & R. E. Hancock. Mechanism of ion transport through the anion-selective channel of the Pseudomonas aeruginosa outer membrane. J Gen Physiol 89, 275-295 (1987)
7. Hancock, R. E., K. Poole, & R. Benz. Outer membrane protein P of Pseudomonas aeruginosa: regulation by phosphate deficiency and formation of small anion-specific channels in lipid bilayer membranes. J Bacteriol 150, 730-738 (1982)
8. Ferenci, T., & W. Boos. The role of the Escherichia col lambda receptor in the transport of maltose and maltodextrins. J Supramol Struct 13, 101-116 (1980)
9. Szmelcman, S., & M. Hofnung. Maltose transport in Escherichia coli K12. Involvement of the bacteriophage lambda receptor. J Bacteriol 124, 112-118 (1975)
10. Werts, C., V. Michel, M. Hofnung, & A. Charbit. Adsorption of bacteriophage lambda on the LamB protein of E. coli K12 : point mutations in gene J of lambda responsible for extended host range. J Bacteriol 176, 941-947 (1994)
11. Charbit, A., & M. Hofnung. Isolation of different bacteriophages using the LamB protein for adsorption on Escherichia coli K12. J Virol 53, 667-671 (1985)
12. Hazelbauer, G. L. Role of the receptor for bacteriophage lambda in the functioning of the maltose chemoreceptor of Escherichia coli. J Bacteriol 124, 119-126 (1975)
13. Hofnung, M., A. Jezierska, & C. Braun-Breton. lamB mutations in E. coli K12: growth of lambda host range mutants and effect of nonsense suppressors. Mol Gen Genet 145, 207-213 (1976)
14. Cowan, S. W., T. Schirmer, G. Rummel, M. Steiert, R. Ghosh, R. A. Pauptit, J. N. Jansonius, & J. P. Rosenbusch. Crystal structures explain functional properties of two E. coli porins. Nature 358, 727-733 (1992)
15. Dutzler, R., G. Rummel, S. Alberti, S. Hernandez-Alles, P. Phale, J. Rosenbusch, V. Benedi, & T. Schirmer. Crystal structure and functional characterization of OmpK36, the osmoporin of Klebsiella pneumoniae. Structure Fold Des 7, 425-434 (1999)
16. Hirsch, A., K. Diederichs, J. Breed, K. Saxena, O. M. Richter, B. Ludwig, & W. Welte. The structure of porin from Paracoccus denitrificans at 3.1 A resolution. FEBS Lett 404, 208-210 (1997)
17. Kreusch, A., A. Neubüser, E. Schiltz, J. Weckesser, & G. E. Schulz. Structure of the membrane channel porin from Rhodopseudomas blastica at 2.0 Å resolution. Protein Sci 3, 58-63 (1994)
18. Weiss, M. S., A. Kreusch, E. Schiltz, U. Nestel, W. Welte, J. Weckesser, & G. E. Schulz. 1991. The structure of porin from Rhodobacter capsulatus at 1.8 Å resolution. FEBS Lett 280:379-382.
19. Zeth, K., K. Diederichs, W. Welte, & H. Engelhardt. Crystal structure of Omp32, the anion-selective porin from Comamonas acidovorans, in complex with a periplasmic peptide at 2.1 A resolution. Structure Fold Des 8, 981-992 (2000)
20. Schirmer, T., T. Keller, Y. F. Wang, & J. P. Rosenbush. Structural basis for sugar translocation through maltoporin channels at 3.5 Å resolution. Science 267, 512-514 (1995)
21. Meyer, J. E. W., M. Hofnung, & G. E. Schulz. Structure of maltoporin from Salmonella typhimurium ligated with a nitrophenyl-maltotrioside. J Mol Biol 266, 761-775 (1997)
22. Forst, D., W. Welte, T. Wacker, & K. Diederichs. Structure of the sucrose-specific porin ScrY from Salmonella typhimurium and its complex with sucrose. Nature Struc Biol 5, 37-46 (1998)
23. Boos, W., & H. Shuman. Maltose/maltodextrin system of Escherichia coli: transport, metabolism, and regulation. Microbiol Mol Biol Rev 62, 204-229 (1998)
24. Randall-Hazelbauer, L., & M. Schwartz. Isolation of the bacteriophage lambda receptor from Escherichia coli. J Bacteriol 116, 1436-1446 (1973)
25. Thirion, J. P., & M. Hofnung. On some genetic aspects of phage lambda resistance in E. coli K12. Genetics 71, 207-216 (1972)
26. Szmelcman, S., & M. Schwartz. Maltose transport in Escherichia coli K12. Eur J Biochem 65, 13-19 (1976)
27. von Meyenburg, K., & H. Nikaido. Outer membrane of gram-negative bacteria. XVII. Secificity of transport process catalyzed by the lambda-receptor protein in Escherichia coli. Biochem Biophys Res Commun 78, 1100-1107 (1977)
28. Luckey, M., & H. Nikaido. Specificity of diffusion channels produced by lambda receptor protein of E. coli. Proc Natl Acad Sci (USA) 77, 167-171 (1980)
29. Bavoil, P., C. Wandersman, M. Schwartz, & H. Nikaido. A mutant form of maltose-binding protein of Escherichia coli deficient in its interaction with the bacteriophage lambda receptor protein. J Bacteriol 155, 919-921 (1983)
30. Neuhaus, J. M., H. Schindler, & J. P. Rosenbusch. The periplasmic maltose-binding protein modifies the channel-forming characteristics of maltoporin. Embo J 2, 1987-1991 (1983)
31. Brass, J. M., M. D. Manson, & T. J. Larson. Transposon Tn10-dependent expression of the lamB gene in Escherichia coli. J Bacteriol 159, 93-99 (1984)
32. Freundlieb, S., U. Ehmann, & W. Boos. Facilitated diffusion of p-Nitrophenyl-□-D-maltohexaoside through the outer membrane of Escherichia coli. J Biol Chem 263, 314-320 (1988)
33. Gehring, K., A. Charbit, E. Brissaud, & M. Hofnung. Bacteriophage lambda receptor site on the Escherichia coli K-12 LamB protein. J Bacteriol 169, 2103-2106 (1987)
34. Francis, G., Brennan, S. Stretton, & T. Ferenci. Genetic mapping of starch -and lambda- receptor sites in maltoporin: identification of substitutions causing direct and indirect effects on binding sites by cysteine mutagenesis. Mol Microbiol 5, 2293-2301 (1991)
35. Charbit, A., C. Werts, V. Michel, P. E. Klebba, P. Quillardet, & M. Hofnung. A role of residue 151 of LamB in bacteriophage lambda adorption: possible steric effect of amino acid substitutions. J Bacteriol 176, 3204-3209 (1994)
36. Charbit, A., K. Gehring, H. Nikaido, T. Ferenci, & M. Hofnung. Maltose transport and starch binding in phage resistant point mutants of maltoporin fuctionnal and topological implications. J Mol Biol 201, 487-496 (1988)
37. Ferenci, T., & K. S. Lee. Channel architecture in maltoporin: dominance studies with lamB mutations influencing maltodextrin binding provide evidence for independent selectivity filters in each subunit. J Bacteriol 171, 855-861 (1989)
38. Heine, H. G., G. Francis, K. S. Lee, & T. Ferenci. Genetic analysis of sequences in maltoporin that contribute to binding domains and pore stucture. J Bacteriol 170, 1730-1738 (1988)
39. Orlik, F., C. Andersen, & R. Benz. 2002. Site-Directed Mutagenesis of Tyrosine 118 within the Central Constriction Site of the LamB (Maltoporin) Channel of Escherichia coli. I. Effect on Ion Transport. Biophys J 82, 2466-2475 (2002)
40. Desaymard, C., M. Debarbouillé, M. Jolit, & M. Schwartz. Mutations affecting antigenic determinants of an outer membrane protein of Escherichia coli. Embo J 5, 1383-1388 (1986)
41. Gabay, J., S. Benson, & M. Schwartz. Genetic mapping of antigenic determinants on a membrane protein. J Biol Chem 258, 2410-2414 (1983)
42. Gabay, J., & M. Schwartz. Monoclonal antibodies as a probe for structure and function of Escherichia coli outer membrane protein. J Biol Chem 257, 6627-6630 (1982)
43. Schenkman, S., E. Couture, & M. Schwartz. Monoclonal antibodies reveal LamB antigenic determinants on both faces of the Escherichia coli outer membrane. J Bacteriol 155, 1382-1392 (1983)
44. Schenkman, S., A. Tsugita, M. Schwartz, & J. P. Rosenbusch. Topology of phage lambda receptor protein. Mapping targets of proteolytic cleavage in relation to binding sites for phage or monoclonal antibodies. J Biol Chem 259, 7570-7576 (1984)
45. Charbit, A., J. C. Boulain, A. Ryter, & M. Hofnung. Probing the topology of a bacterial membrane protein by genetic insertion of a foreign epitope; Expression at the cell surface. Embo J 5, 3029-3037 (1986)
46. Charbit, A., J. Ronco, V. Michel, C. Werts, & M. Hofnung. Permissive sites and the topology of an outer-membrane protein with a reporter epitope. J Bacteriol 173, 262-275 (1991)
47. Newton, S. M. C., P. E. Klebba, V. Michel, M. Hofnung, & A. Charbit. Topology of the membrane protein LamB by epitope tagging and a comparison with the X-ray model. J Bacteriol 178, 3447-3456 (1996)
48. Charbit, A., J. Wang, V. Michel, & M. Hofnung. A cluster of charged and aromatic residues in the C-terminal portion of maltoporin participates in sugar binding and uptake. Mol Gen Genet 260, 185-92 (1998)
49. Klebba, P., E., S. Newton, M. C., A. Charbit, V. Michel, D. Pérrin, & D. Hofnung. Further genetic analysis of the C-terminal loop region in Escherichia coli maltoporin. Res Microbiol 148, 375-387 (1997)
50. Klebba, P. E., M. Hofnung, & A. Charbit. Mechanism of maltodextrin transport through the sugar-specific porin, LamB. Embo J 13, 4670-4675 (1994)
51. Andersen, C., C. Bachmeyer, H. Tauber, R. Benz, J. Wang, V. Michel, S. M. Newton, M. Hofnung, & A. Charbit. In vivo and in vitro studies of major surface loop deletion mutants of the Escherichia coli K12 maltoporin: contribution to maltose and maltooligosaccharide transport and binding. Mol Microbiol 32, 851-867 (1999)
52. Benz, R., G. Francis, T. Nakae, & T. Ferenci. Investigation of the selectivity of maltoporin channels using mutant LamB proteins: mutations changing the maltodextrin binding site. Biochimica and Biophysica Acta 1104, 299-307 (1992)
53. Jordy, M., C. Andersen, K. Schulein, T. Ferenci, & R. Benz. Rate constants of sugar transport through two LamB mutants of Escherichia coli: comparison with wild-type maltoporin and LamB of Salmonella typhimurium. J Mol Biol 259, 666-678 (1996)
54. Dumas, F., R. Koebnik, M. Winterhalter, & P. Van Gelder. Sugar transport through maltoporin of Escherichia coli. Role of polar tracks. J Biol Chem 275, 19747-19751 (2000)
55. Dutzler, R., Y. F. Wang, P. Rizkallah, J. P. Rosenbusch, & T. Schirmer. Crystal structures of various malto-oligosaccharides bound to maltoporin reveal a specific sugar translocation pathway. Structure 4, 127-34 (1996)
56. Van Gelder, P., F. Dumas, I. Bartoldus, N. Saint, A. Prilipov, M. Winterhalter, Y. Wang, A. Philippsen, J. P. Rosenbusch, & T. Schirmer. Sugar transport through maltoporin of Escherichia coli: role of the greasy slide. J Bacteriol 184, 2994-2999 (2002)
57. Clément, J-M., &d M. Hofnung. Gene sequence of the lambda receptor, an outer membrane protein of E. coli K12. Cell 27, 507-514 (1981)
58. Schneider, E., S. Freundlieb, S. Tapio, & W. Boos. Molecular characterization of the MalT-dependent periplasmic alpha-amylase of Escherichia coli encoded by malS. J Biol Chem 267, 5148-5154 (1992)
59. Benz, R., A. Schmid, & G. H. Vos-Scheperkeuter. Mechanism of sugar transport through the sugar-specific LamB channel of Escherichia coli outer membrane. J Membr Biol 100, 21-29 (1987)
60. Boos, W., U. Ehmann, H. Forkl, W. Klein, M. Rimmele, & P. Postma. Trehalose transport and metabolism in Escherichia coli. J Bacteriol 172, 3450-3461 (1990)
61. Klein, W., & W. Boos. Induction of the lambda receptor is essential for effective uptake of trehalose in Escherichia coli. J Bacteriol 175, 1682-1686 (1993)
62. Schmid, K., R. Ebner, K. Jahreis, J. W. Lengeler, & F. Titgemeyer. A Sugar-Specific Porin, ScrY, Is Involved in Sucrose Uptake in Enteric Bacteria. Mol Microbiol 5, 941-950 (1991)
63. Schülein, K., K. Schmid, & R. Benz. The sugar-specific outer membrane channel ScrY contains functional characteristics of general diffusion pores and substrate-specific porins. Mol Microbiol 5, 2233-2241 (1991)
64. Schülein, K., C. Andersen, & R. Benz. The deletion of 70 amino acids near the N-terminal end of the sucrose porin Scry causes its functional similarity to LamB in vivo and in vitro. Mol Microbiol 17, 757-767 (1995)
65. Andersen, C., B. Schiffler, A. Charbit, & R. Benz. PH-induced collapse of the extracellular loops closes Escherichia coli maltoporin and allows the study of asymmetric sugar binding. J Biol Chem 277, 41318-25 (2002)
66. Dutzler, R., T. Schirmer, M. Karplus, & S. Fischer. Translocation mechanism of long sugar chains across the maltoporin membrane channel. Structure (Camb) 10, 1273-84 (2002)