A Porin Like Outer Membrane Protein (Omp26La) Appears to Increase in an Oxytetracycline Resistant Strain of Marine Fish Pathogen Vibrio (Listonella) anguillarum.

Yasue, Kazushige; Kusuda, Riichi

doi:10.1264/jsme2.13.197

Cited by 5 publications

(4 citation statements)

References 12 publications

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“…The N-terminal 10 amino acids of the protein purified from the wild type (slow migrating) and mutant (fast migrating) were identical to each other and to the deduced amino acid sequence of the OmpU protein (62). The 10 N-terminal amino acids of the overexpressed band marked V were identical to the previously identified OmpV protein (53).…”

Section: Vol 73 2005 Lps-o1 Side Chain Iron Transport and Virulensupporting

confidence: 50%

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Novel Role of the Lipopolysaccharide O1 Side Chain in Ferric Siderophore Transport and Virulence of Vibrio anguillarum

Welch

Crosa

2005

Infect Immun

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From a library of approximately 20,000 transposon mutants, we have identified mutants affected in chromosomal genes involved in synthesis of the siderophore anguibactin, as well as in ferric anguibactin utilization. Genetic and sequence analyses of one such transport-defective mutant revealed that the transposon insertion occurred in an open reading frame (ORF) with homology to rmlC, a dTDP-rhamnose biosynthetic gene. This ORF resides within a cluster of four ORFs, all of which are predicted to function in the biosynthesis of this O side chain precursor. The same phenotype was seen in a mutant obtained by allelic exchange in rmlD, another ORF in this dTDP-rhamnose biosynthetic cluster. This mutation could be complemented with the wild-type rmlD gene, restoring both production of the O1 antigen side chain and ferric anguibactin transport. Presence of the O1 side chain was crucial for the resistance of Vibrio anguillarum to the bactericidal action of nonimmune serum from the fish host. Surprisingly, further analysis demonstrated that these mutations were pleiotropic, leading to a dramatic decrease in the levels of FatA, the outer membrane protein receptor for ferric anguibactin transport, and a concomitant reduction in iron transport. Thus, our results in this work demonstrate that the lipopolysaccharide O1 side chain is required for the operation of two critical virulence factors in V. anguillarum: serum resistance and anguibactin-mediated iron transport. These factors allow V. anguillarum to survive in serum and multiply in the iron-limiting milieu of the host vertebrate.

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Section: Vol 73 2005 Lps-o1 Side Chain Iron Transport and Virulensupporting

confidence: 50%

“…OmpV has also been found to be overexpressed in an oxytetracycline-resistant strain of V. anguillarum (53). A homologue of this protein has also been reported in V. cholerae (41,54).…”

Section: Discussionmentioning

confidence: 88%

Novel Role of the Lipopolysaccharide O1 Side Chain in Ferric Siderophore Transport and Virulence of Vibrio anguillarum

Welch

Crosa

2005

Infect Immun

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“…4). Omp26La is a porin-like OMP first cloned by Suzuki et al (1998). Because of limited research information, the biological function of Omp26La remains unknown.…”

Section: Survival (Log Cfu MLmentioning

confidence: 99%

Salt-responsive outer membrane proteins ofVibrio anguillarumserotype O1 as revealed by comparative proteome analysis

Kao

Cheng

Kuo

et al. 2009

Journal of Applied Microbiology

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Aims: Vibrio anguillarum is a universal marine pathogen causing vibriosis. Vibrio anguillarum encounters different osmolarity conditions between seawater and hosts, and its outer membrane proteins (OMPs) play a crucial role in the adaptation to changes of the surroundings. In the present study, proteomic approaches were applied to investigate the salt‐responsive OMPs of V. anguillarum. Methods and Results: Lower salinity (0·85% NaCl) is more suitable for growth, survival and swimming motility of the bacterium. Comparative two‐dimensional electrophoresis (2‐DE) analysis reveals six differentially expressed protein spots among three different salinities, which were successfully identified as OmpU, maltoporin, flagellin B, Omp26La, Omp26La and OmpW respectively. Conclusions: OmpW and OmpU were highly expressed at 3·5% salinity, suggesting their role in the efficient efflux of NaCl. Maltoporin was downregulated in higher salinity, indicating that higher osmolarity inhibits carbohydrate transport and bacterial growth. Omp26La, the homologue of OmpV, functions as a salt‐responsive protein in lower salinity. Significance and Impact of the Study: To the best of our knowledge, this is the first report describing salt stress‐responsive proteins of V. anguillarum using proteomic approaches. Our results provide a useful strategy for delineating the osmoregulatory mechanism of the marine pathogens.

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“…These two proteins are homologs of each other and the outer membrane protein OmpV in V. cholerae (Pohlner et al 1986). Ψ‐BLAST also reveals that these proteins are homologous to a porin‐like outer membrane protein Omp26La in L. anguillarum (Table 2; Suzuki et al 1998). The functions of YiaT and YeaF are currently unknown, but the analyses of our program show that they may be of β‐barrel structure.…”

Section: Resultsmentioning

confidence: 99%

The β‐barrel finder (BBF) program, allowing identification of outer membrane β‐barrel proteins encoded within prokaryotic genomes

2002

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Many outer membrane proteins (OMPs) in Gram-negative bacteria possess known ␤-barrel three-dimensional (3D) structures. These proteins, including channel-forming transmembrane porins, are diverse in sequence but exhibit common structural features. We here report computational analyses of six outer membrane proteins of known 3D structures with respect to (1) secondary structure, (2) hydropathy, and (3) amphipathicity. Using these characteristics, as well as the presence of an N-terminal targeting sequence, a program was developed allowing prediction of integral membrane ␤-barrel proteins encoded within any completely sequenced prokaryotic genome. This program, termed the ␤-barrel finder (BBF) program, was used to analyze the proteins encoded within the Escherichia coli genome. Out of 4290 sequences examined, 118 (2.8%) were retrieved. Of these, almost all known outer membrane proteins with established ␤-barrel structures as well as many probable outer membrane proteins were identified. This program should be useful for predicting the occurrence of outer membrane proteins in bacteria with completely sequenced genomes.

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A Porin Like Outer Membrane Protein (Omp26La) Appears to Increase in an Oxytetracycline Resistant Strain of Marine Fish Pathogen Vibrio (Listonella) anguillarum.

Cited by 5 publications

References 12 publications

Novel Role of the Lipopolysaccharide O1 Side Chain in Ferric Siderophore Transport and Virulence of Vibrio anguillarum

Novel Role of the Lipopolysaccharide O1 Side Chain in Ferric Siderophore Transport and Virulence of Vibrio anguillarum

Salt-responsive outer membrane proteins ofVibrio anguillarumserotype O1 as revealed by comparative proteome analysis

The β‐barrel finder (BBF) program, allowing identification of outer membrane β‐barrel proteins encoded within prokaryotic genomes

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