Bacterial Receptors for Phages and Colicins as Constituents of Specific Transport Systems

Braun, Volkmar; Hantke, Klaus

doi:10.1007/978-1-4615-9698-1_3

Cited by 34 publications

(21 citation statements)

References 112 publications

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“…Genetic evidence suggests that essentially the same site on the lamB protein may be interacting with phage X or the host-range mutants of phage Tula. The primary recognition of a bacterium by a bacteriophage involves the interaction of the phage with a specific structure, called the receptor, located at the bacterial surface (1). Numerous phage receptors have now been chemically identified (1)(2)(3) on the basis of evidence that (i) they interact with the phage in vitro (ii) they are absent or altered in bacterial mutants resistant to the phage. Such identifications were possible only because the phages involved in these studies could recognize a single kind of receptor, and could therefore no longer adsorb when this receptor was not present at the bacterial surface.…”

mentioning

confidence: 99%

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

Wandersman¹,

Schwartz²

1978

Proc. Natl. Acad. Sci. U.S.A.

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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 X. Datta et al [Datta, D. B., Arden, B. & Henning, U. (1977) J. Bacteriol. 131, 821-8291 recently isolated a phage called Tula that uses protein Ia for its adsorption. While phage Tula fails to grow on ompB mutants, which lack rotein Ia, we show here that host-range mutants of Tula 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 there 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 X or the host-range mutants of phage Tula. The primary recognition of a bacterium by a bacteriophage involves the interaction of the phage with a specific structure, called the receptor, located at the bacterial surface (1). Numerous phage receptors have now been chemically identified (1-3) on the basis of evidence that (i) they interact with the phage in vitro (ii) they are absent or altered in bacterial mutants resistant to the phage. Such identifications were possible only because the phages involved in these studies could recognize a single kind of receptor, and could therefore no longer adsorb when this receptor was not present at the bacterial surface. We wish to report a case in which, in apparent contradiction to this general rule, a phage seems able to use either of two different outer membrane proteins to adsorb to Escherichia coli K-12 cells.The lamB protein (molecular weight about 50,000) is a component of the transport system for maltose and maltodextrins (4), facilitating the diffusion of these substrates across the outer membrane (5). The protein is also-and was in fact first recognized as-the receptor for phage X (6). All the genetic (7-9) and biochemical (6, 10, 11) evidence suggests that this protein indeed is the receptor-i.e., that it bears all the chemical determinants required for recognition of the bacterial surface by this phage. The lamB gene is part of the maltose regulon (7,12,13) (19,20). Present evidence does not allow one to decide whether tolF or ompB is the structural gene for this protein (21). Phage Tula fails to grow on ompB strains, which lack detectable amounts of protein Ia (18,19).The experiments reported in this paper indicate that some host range mutants of phage Tula can use either protein Ia or the lamB protein to adsorb to E. coli cells.MATERIALS AND METHODS The bacterial strains are listed in Table 1. The strains of phage X-i.e., XV, XVho, and XVh4h*16 are all described in ref. 9, and will be referred to respectively as X, Xh, and Xhh*. Phage Tula (18) was kindly sent to us by U. Henning. Phage TP1, a host range mutant of Tula, will be described in this paper.All media and standard techniques were previously described (22). Spontaneous mutants re...

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mentioning

confidence: 99%

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

Wandersman¹,

Schwartz²

1978

Proc. Natl. Acad. Sci. U.S.A.

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“…Two additional proteins, ExbB and ExbD also play a role in TonB-dependent uptake of colicin M [47]. All ExbBD related functions (uptake of growth factors and colicins) are also TonB dependent processes.…”

Section: Receptor Binding and Coficin Uptakementioning

confidence: 99%

The biology of colicin M

Harkness¹

1991

FEMS Microbiology Letters

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“…These pores are constructed from three identical subunits of the outer membrane proteins, known as porins (5,11). Thus, the pores made of porins play a major role in the translocation of solutes across the outer membrane, with the exception of certain specific solutes (3,14). Small hydrophilic antibiotics such as 1-lactams are believed to diffuse through porin pores (13).…”

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confidence: 99%

Diffusion of beta-lactam antibiotics through liposome membranes containing purified porins

Kobayashi¹,

Takahashi²,

Nakae³

1982

Antimicrob Agents Chemother

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A method to determine the diffusion of cephalosporins through porin pores in vitro was developed, using liposomes reconstituted from phospholipids, lipopolysaccharides, and purified porin trimers. With this method, the roles of several species of porin pores from Escherichia coli and Salmonella typhimurium in the diffusion of cephalexin, cephaloridine, and cephalothin were examined. Results clearly showed that porins from E. coli B and 39,000-molecular-weight porins from S. typhimurium formed the most efficient pores. Thus, these were considered to represent a single functional group. OmpF and OmpE porins of E. coli K-12 and 38,000-molecular-weight porins of S. typhimurium formed moderately efficient pores. OmpC porins of E. coli K-12 and 40,000-molecular-weight porins of S. typhimurium were the least efficient pore formers. The present method can be used to distinguish the role of individual porin pores in the diffusion of cephalosporins.

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Bacterial Receptors for Phages and Colicins as Constituents of Specific Transport Systems

Cited by 34 publications

References 112 publications

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

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

The biology of colicin M

Diffusion of beta-lactam antibiotics through liposome membranes containing purified porins

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