A common receptor protein for phage T5 and colicin M in the outer membrane of Escherichia coli B

Braun, Volkmar; Schaller, Klaus; Wolff, Helga

doi:10.1016/0005-2736(73)90433-1

Cited by 177 publications

(119 citation statements)

References 34 publications

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“…This may explain the observation that X can transduce strains with a deletion of the lamB gene at low efficiency (14). Phage T5 has two sets of tail fibers, the L-shaped tail fibers, the product of the ltf gene, which bind to the lipopolysaccharide, and a single straight terminal tail fiber, the product of the oad gene, which binds to the FhuA receptor protein (13,39,40). The L-shaped tail fibers accelerate adsorption, but neither the L-shaped tail fibers nor the lipopolysaccharide receptor are essential for infection (39,40,79).…”

Section: Resultsmentioning

confidence: 99%

DNA sequences of the tail fiber genes of bacteriophage P2: evidence for horizontal transfer of tail fiber genes among unrelated bacteriophages

1992

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We have determined the DNA sequence of the bacteriophage P2 tail genes G and H, which code for polypeptides of 175 and 669 residues, respectively. Gene H probably codes for the distal part of the P2 tail fiber, since the deduced sequence of its product contains regions similar to tail fiber proteins from phages Mu, P1, lambda, K3, and T2. The similarities of the carboxy-terminal portions of the P2, Mu, ann P1 tail fiber proteins may explain the observation that these phages in general have the same host range. The P2 H gene product is similar to the products of both lambda open reading frame (ORF) 401 (stf, side tail fiber) and its downstream ORF, ORF 314. If 1 bp is inserted near the end of ORF 401, this reading frame becomes fused with ORF 314, creating an ORF that may represent the complete stf gene that encodes a 774-amino-acid-long side tail fiber protein. Thus, a frameshift mutation seems to be present in the common laboratory strain of lambda. Gene G of P2 probably codes for a protein required for assembly of the tail fibers of the virion. The entire G gene product is very similar to the products of genes U and U' of phage Mu; a region of these proteins is also found in the tail fiber assembly proteins of phages TuIa, TuIb, T4, and lambda. The similarities in the tail fiber genes of phages of different families provide evidence that illegitimate recombination occurs at previously unappreciated levels and that phages are taking advantage of the gene pool available to them to alter their host ranges under selective pressures.

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Section: Resultsmentioning

confidence: 99%

DNA sequences of the tail fiber genes of bacteriophage P2: evidence for horizontal transfer of tail fiber genes among unrelated bacteriophages

1992

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“…In this context, the Siphoviridae coliphage T5 is a very suitable model: its tail tip is composed of a limited number of proteins, as noted in the accompanying article by Zivanovic et al (11) (Fig. 1A and B), and its protein receptor has been identified as FhuA, the outer membrane iron-ferrichrome transporter (12). The phage T5 adsorption device contains three L-shaped fibers attached to a conical structure that is extended by a straight fiber, at the tip of which is located only one copy of the RBP (Fig.…”

mentioning

confidence: 99%

Crystal Structure of pb9, the Distal Tail Protein of Bacteriophage T5: a Conserved Structural Motif among All Siphophages

Flayhan

Vellieux

Lurz

et al. 2014

J Virol

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fThe tail of Caudovirales bacteriophages serves as an adsorption device, a host cell wall-perforating machine, and a genome delivery pathway. In Siphoviridae, the assembly of the long and flexible tail is a highly cooperative and regulated process that is initiated from the proteins forming the distal tail tip complex. In Gram-positive-bacterium-infecting siphophages, the distal tail (Dit) protein has been structurally characterized and is proposed to represent a baseplate hub docking structure. It is organized as a hexameric ring that connects the tail tube and the adsorption device. In this study, we report the characterization of pb9, a tail tip protein of Escherichia coli bacteriophage T5. By immunolocalization, we show that pb9 is located in the upper part of the cone of the T5 tail tip, at the end of the tail tube. The crystal structure of pb9 reveals a two-domain protein. Domain A exhibits remarkable structural similarity with the N-terminal domain of known Dit proteins, while domain B adopts an oligosaccharide/ oligonucleotide-binding fold (OB-fold) that is not shared by these proteins. We thus propose that pb9 is the Dit protein of T5, making it the first Dit protein described for a Gram-negative-bacterium-infecting siphophage. Multiple sequence alignments suggest that pb9 is a paradigm for a large family of Dit proteins of siphophages infecting mostly Gram-negative hosts. The modular structure of the Dit protein maintains the basic building block that would be conserved among all siphophages, combining it with a more divergent domain that might serve specific host adhesion properties.

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“…The adsorption of bacteriophage T5 to the surface of Escherichia coli F (35) is characterized by two specific steps: (i) reversible binding to the polymannose 0 antigen (17,18) and (ii) itreversible binding to the FhuA receptor protein involved in ferrichrome-iron transport (3,26). Binding to the O antigen is mediated by the L-shaped tail fibers and accelerates adsorption by a factor of 15 (17).…”

mentioning

confidence: 99%

Cloning, sequencing, and recombinational analysis with bacteriophage BF23 of the bacteriophage T5 oad gene encoding the receptor-binding protein

Krauel

Heller

1991

J Bacteriol

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Binding of bacteriophage T5 to its receptor, the Escherichia coli FhuA protein, is mediated by tail protein pb5. In this article we confirm that pb5 is encoded by the T5 oad gene and describe the isolation, expression, and sequencing of this gene. In order to locate oad precisely, we analyzed recombinants between BF23, a T5-related phage with a different host range, and plasmid clones containing segments of the T5 chromosome. This analysis also showed that oad has little or no homology with hrs, the analogous BF23 gene. We were able to overproduce a protein that comigrates with pb5 after fusing a 2-kb segment containing oad to a phage T7

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A common receptor protein for phage T5 and colicin M in the outer membrane of Escherichia coli B

Cited by 177 publications

References 34 publications

DNA sequences of the tail fiber genes of bacteriophage P2: evidence for horizontal transfer of tail fiber genes among unrelated bacteriophages

DNA sequences of the tail fiber genes of bacteriophage P2: evidence for horizontal transfer of tail fiber genes among unrelated bacteriophages

Crystal Structure of pb9, the Distal Tail Protein of Bacteriophage T5: a Conserved Structural Motif among All Siphophages

Cloning, sequencing, and recombinational analysis with bacteriophage BF23 of the bacteriophage T5 oad gene encoding the receptor-binding protein

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