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

Krauel, Verena; Heller, Knut J.

doi:10.1128/jb.173.3.1287-1297.1991

Cited by 21 publications

(34 citation statements)

References 64 publications

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“…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). The oad gene, which encodes the terminal receptor binding protein of T5, has been sequenced (54); the oad gene product shows no similarity to any of the tail fiber proteins or to any other protein in the data bases (data not shown).…”

Section: Resultsmentioning

confidence: 99%

“…5E) and from 41 to 84% identity for region T (about 154 residues in length). [93], P2 H [66] K3 37 [100], Ml 37 [45], Ox2 37 [45] K3 38 [63], Ml 38 [50] [62], K3 37 [54], T2 37 [53] TuIb 37 [91], Tula 37 [85], X Stf [76], e14 ORF Pmin [36] Tula 37 [47], TuIb 37 [47], X Stf [41] T3 Tf [87] T3 Tf [90], K3 37 [29] T3 Tf [39] T2 37 [61], T4 37 [60] K3 37 [69], T2 37 [68], T4 37 [62] TuIb 37 [88], T4 37 [85], X Stf [72], e14 ORF Pmin [36] TuIb 37 [84], X Stf [58], T4 37 [47] T4 37 [91], Tula 37 [88], X Stf [73], e14 ORF Pmin [36] Tula 37 ...…”

Section: Resultsmentioning

confidence: 99%

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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%

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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“…Binding to FhuA is not mediated by the pb2 straight tail fiber protein of T5 but by pb5 (36,39,45). pb5 is not located at the tip of the tail (39), as one might expect, but rather 50 nm distant from the extremity of the straight tail fiber (1).…”

Section: Interaction Of Phage T5 With the Fhua Receptor Proteinmentioning

confidence: 99%

FhuA (TonA), the Career of a Protein

Braun

2009

J Bacteriol

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The interest in the TonA protein, now called FhuA, has endured since the beginnings of phage genetics and molecular biology. The functions of this energy-coupled transporter and receptor in the outer membrane of Escherichia coli cells are fascinating. The historical perspective of this protein presented here is not intended to provide a comprehensive account of the structure and function of FhuA but rather attempts to explain how this protein has attracted interest for so long.The seminal work published by Salvador E. Luria and Max Delbrück (51) in 1943 is considered the beginning of modern bacterial genetics (12). In this publication, they reported their fluctuation test, which demonstrates that in bacteria, genetic mutations arise in the absence of selection rather than as a response to selection. They isolated virus-resistant mutants of Escherichia coli B, ascribed this virus resistance to mutations in the host cells prior to infection by the phage, and presented a means for quantitatively calculating mutation rates. The virus they used was later named phage T1, and the mutations that conferred resistance were subsequently designated tonA and tonB (ton derived from T one). It was later found that a phage morphologically and serologically distinct from T1, named T5, cannot infect tonA mutants but can infect tonB mutants; i.e., phage T5 requires only the tonA-encoded function but not the tonB-encoded function.Members of the "phage group" surrounding Luria and Delbrück were interested in genetics, reproduction, and multiplication. They studied, as the most simple system, phages and E. coli host cells, mutants, phage morphology, serology, adsorption, lysis, and burst size, but not biochemistry (12,14). The prejudice against biochemistry began to dissolve during the postdoctoral studies of Wolfhard Weidel, a biochemist by training, on phage adsorption and infection in Delbrück's laboratory. Delbrück's enthusiasm for Weidel's studies was evident in his report to the Caltech president, in which he referred to Weidel's work as "the most startling finding of the year" (66). Weidel's findings were included in the 1950 report on viruses of the Division of Biology of the California Institute of Technology. They were published in 1951 (68) after he was back in Germany at the Max Planck Institute of Biology in Tübingen, where he continued his work on phage adsorption, first with phages T2, T4, and T6 and then mainly with phage T5. His first achievement was the isolation of membrane fractions from E. coli B that bound the T phages with kinetics resembling those obtained with living bacteria. He could differentiate between receptors for T2, T4, and T6 on the one side and phage T5 on the other side. Electron microscopy revealed phage-induced degradation of the cell envelopes (68), which was later assigned to the T2 lysozyme (69).The methods used at that time were rather crude. The T5 receptor was extracted from cells by treatment with 0.1 N NaOH, neutralized with CO 2 , precipitated with 20% acetic acid, and then solubilized ...

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“…Sequence data for BF23 is incomplete, but the genes that encode some of its tail proteins are known and sequenced (62,63). Blast analyses of H8 DNA identified ORFs at 94.7 kb and 82.8 kb that encode homologous proteins to the experimentally demonstrated receptor binding proteins of BF23 (Hrs) (48) and T5 (pb5, encoded by oad) (39, 63) and the pore-forming tail proteins of T5 (pb2) (7,28), respectively. The receptor binding protein (encoded by rbp) of H8 was one of the least conserved in the genome, relative to its T5 homolog (26% identity; 41% similarity).…”

Section: /67mentioning

confidence: 99%

FepA- and TonB-Dependent Bacteriophage H8: Receptor Binding and Genomic Sequence

Rabsch

Wiley

et al. 2007

J Bacteriol

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H8 is derived from a collection of Salmonella enterica serotype Enteritidis bacteriophage. Its morphology and genomic structure closely resemble those of bacteriophage T5 in the family Siphoviridae. H8 infected S. enterica serotypes Enteritidis and Typhimurium and Escherichia coli by initial adsorption to the outer membrane protein FepA. Ferric enterobactin inhibited H8 binding to E. coli FepA (50% inhibition concentration, 98 nM), and other ferric catecholate receptors (Fiu, Cir, and IroN) did not participate in phage adsorption. H8 infection was TonB dependent, but exbB mutations in Salmonella or E. coli did not prevent infection; only exbB tolQ or exbB tolR double mutants were resistant to H8. Experiments with deletion and substitution mutants showed that the receptor-phage interaction first involves residues distributed over the protein's outer surface and then narrows to the same charged (R316) or aromatic (Y260) residues that participate in the binding and transport of ferric enterobactin and colicins B and D. These data rationalize the multifunctionality of FepA: toxic ligands like bacteriocins and phage penetrate the outer membrane by parasitizing residues in FepA that are adapted to the transport of the natural ligand, ferric enterobactin. DNA sequence determinations revealed the complete H8 genome of 104.4 kb. A total of 120 of its 143 predicted open reading frames (ORFS) were homologous to ORFS in T5, at a level of 84% identity and 89% similarity. As in T5, the H8 structural genes clustered on the chromosome according to their function in the phage life cycle. The T5 genome contains a large section of DNA that can be deleted and that is absent in H8: compared to T5, H8 contains a 9,000-bp deletion in the early region of its chromosome, and nine potentially unique gene products. Sequence analyses of the tail proteins of phages in the same family showed that relative to pb5 (Oad) of T5 and Hrs of BF23, the FepA-binding protein (Rbp) of H8 contains unique acidic and aromatic residues. These side chains may promote binding to basic and aromatic residues in FepA that normally function in the adsorption of ferric enterobactin. Furthermore, a predicted H8 tail protein showed extensive identity and similarity to pb2 of T5, suggesting that it also functions in pore formation through the cell envelope. The variable region of this protein contains a potential TonB box, intimating that it participates in the TonB-dependent stage of the phage infection process.Bacteriophage adsorb to components of the gram-negative bacterial outer membrane (OM) during the initial stages of their infectious processes (17,20,36,37,64,87,88,98). For example, phages Mu (84) and X174 (41) initially bind to lipopolysaccharide, whereas (95), T6 (86), and TLS (30) adsorb to the OM proteins LamB, Tsx, and TolC, respectively. T2 (53) and T4 (92, 102) utilize both lipopolysaccharide and surface proteins in their adsorption reactions. The surface receptor proteins are porins that nonspecifically (70, 71) or specifically (55, 56, 69) transport...

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

Cited by 21 publications

References 64 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

FhuA (TonA), the Career of a Protein

FepA- and TonB-Dependent Bacteriophage H8: Receptor Binding and Genomic Sequence

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