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

Abstract

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...

New locus (ttr) in Escherichia coli K-12 affecting sensitivity to bacteriophage T2 and growth on oleate as the sole carbon source

“…Exceptions are known in which a phage can use two or three different outer membrane proteins as receptors. This has been demonstrated by the use of mutant strains deficient in one or more well-characterized outer membrane proteins and by the isolation of resistant mutants in strains already lacking one of the receptor proteins (3,21,23,37).…”

“…The receptor affected by ttr was the major receptor used by phage T2 and was located in the outer membrane. (3,21,23,37).In this communication we describe an analysis of strains resistant to phage T2. This phage has been reported to use the outer membrane protein OmpF as its receptor (10), since phage T2-resistant mutants have reduced amounts of or lack this protein, and also purified OmpF protein and lipopolysaccharide are able to neutralize the phage.…”

“…The receptor affected by ttr was the major receptor used by phage T2 and was located in the outer membrane. (3,21,23,37).…”

The levanase operon of Bacillus subtilis expressed in Escherichia coli can substitute for the mannose permease in mannose uptake and bacteriophage lambda infection

“…In addition, we tested several phages by using outer membrane proteins other than LamB as cell surface receptors; these phages included (i) cI57h434, a recombinant between (cI57) and phage 434 with the immunity of and the host range of 434, using the outer membrane protein OmpC as a receptor (2); (ii) phage Tu 1a (7), using OmpF as a receptor; (iii) phage Tu II*, using OmpA as a receptor; and (iv) two phages that are alternate users of either LamB or OmpF (TP1) (40) and either LamB or OmpC (AB48) (4).…”

“…Strikingly, the mutation in the IID Man subunit in ZSC113 had only very little, if any, effect on infection by this phage. We finally tested as controls (not included in Table 2) the sensitivity of the Pel ϩ strain 921 and the Pel Ϫ strain WA2127 to four other non--like phages: phage Tu1a (using OmpF as the surface receptor), phage TuII* (using OmpA) (7), and two phages, TP1 and AB48 (using either LamB or OmpF and either LamB or OmpC, respectively) (4,40). The EOP of the four phages was identical on the two E. coli strains, indicating that these phages do not require the PTS proteins for infection.…”