Identification of a segment of the Escherichia coli Tsx protein that functions as a bacteriophage receptor area

Schneider, Hans Joachim; Fsihi, Hafida; Kottwitz, Brunhilde; Mygind, Benete; Bremer, Erhard

doi:10.1128/jb.175.10.2809-2817.1993

Cited by 17 publications

(22 citation statements)

References 41 publications

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“…ictaluri phage susceptibility. These results showed striking similarities with a previous finding that demonstrated that alterations clustered in a small region near the surface-exposed carboxy terminus of Tsx protein resulted in Tsx-specific phage-resistance phenotypes (Schneider et al, 1993). The involvement of other surface-exposed regions in phage attachment is not unexpected as it has been demonstrated by mutational analysis of several phage receptors (Cole et al, 1983;Gehring et al, 1987;Heine et al, 1988).…”

Section: Discussionsupporting

confidence: 78%

An outer membrane porin protein modulates phage susceptibility in Edwardsiella ictaluri

et al. 2012

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Bacteriophages WeiAU and WeiDWF are lytic to the catfish pathogen Edwardsiella (Edw.) ictaluri. The Edw. ictaluri host factors that modulate phage-host interactions have not been described previously. This study identified eleven unique Edw. ictaluri host factors essential for phage infection by screening a transposon mutagenized library of two Edw. ictaluri strains for phageresistant mutants. Two mutants were isolated with independent insertions in the ompLC gene that encodes a putative outer membrane porin. Phage binding and efficiency of plaquing assays with Edw. ictaluri EILO, its ompLC mutant and a complemented mutant demonstrated that OmpLC serves as a receptor for phage WeiAU and WeiDWF adsorption. Comparison of translated OmpLCs from 15 Edw. ictaluri strains with varying degrees of phage susceptibility revealed that amino acid variations were clustered on the predicted extracellular loop 8 of OmpLC. Deletion of loop 8 of OmpLC completely abolished phage infectivity in Edw. ictaluri. Site-directed mutagenesis and transfer of modified ompLC genes to complement the ompLC mutants demonstrated that changes in ompLC sequences affect the degree of phage susceptibility. Furthermore, Edw. ictaluri strain Alg-08-183 was observed to be resistant to WeiAU, but phage progeny could be produced if phage DNA was electroporated into this strain. A host-range mutant of WeiAU, WeiAU-183, was isolated that was capable of infecting strain Alg-08-183 by using OmpLC as a receptor for adsorption. The results of this study identified Edw. ictaluri host factors required for phage infection and indicated that OmpLC is a principal molecular determinant of phage susceptibility in this pathogen.

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Section: Discussionsupporting

confidence: 78%

An outer membrane porin protein modulates phage susceptibility in Edwardsiella ictaluri

et al. 2012

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“…OmpF has been known to comigrate with OmpC on SDS-PAGE gels (5,37). We performed Western blotting analysis to ascertain that the changes in cellular OmpC concentration can be reflected by the fluctuating intensity of the 33-kDa protein band.…”

Section: Ar1-resistant Mutants Obtained By Transposon Mutagenesismentioning

confidence: 99%

Characterization of the Distal Tail Fiber Locus and Determination of the Receptor for Phage AR1, Which Specifically Infects Escherichia coli O157:H7

Yu¹,

Ko²,

Chen³

et al. 2000

J Bacteriol

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Phage AR1 is similar to phage T4 in several essential genes but differs in host range. AR1 infects various isolates of Escherichia coli O157:H7 but does not infect K-12 strains that are commonly infected by T4. We report here the determinants that confer this infection specificity. In T-even phages, gp37 and gp38 are components of the tail fiber that are critical for phage-host interaction. The counterparts in AR1 may be similarly important and, therefore, were characterized. The AR1 gp37 has a sequence that differs totally from those of T2 and T4, except for a short stretch at the N terminus. The gp38 sequence, however, has some conservation between AR1 and T2 but not between AR1 and T4. The sequences that are most closely related to the AR1 gp37 and gp38 are those of phage Ac3 in the T2 family. To identify the AR1-specific receptor, E. coli O157:H7 was mutated by Tn10 insertion and selected for an AR1-resistant phenotype. A mutant so obtained has an insertion occurring at ompC that encodes an outer membrane porin. To confirm the role of OmpC in the AR1 infection, homologous replacement was used to create an ompC disruption mutant (RM). When RM was complemented with OmpC originated from an O157:H7 strain, but not from K-12, its AR1 susceptibility was fully restored. Our results suggest that the host specificity of AR1 is mediated at least in part through the OmpC molecule.

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“…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.…”

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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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Identification of a segment of the Escherichia coli Tsx protein that functions as a bacteriophage receptor area

Cited by 17 publications

References 41 publications

An outer membrane porin protein modulates phage susceptibility in Edwardsiella ictaluri

An outer membrane porin protein modulates phage susceptibility in Edwardsiella ictaluri

Characterization of the Distal Tail Fiber Locus and Determination of the Receptor for Phage AR1, Which Specifically Infects Escherichia coli O157:H7

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

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