Role for the major outer-membrane protein from Vibrio anguillarum in bile resistance and biofilm formation

Wang, Suyan; Lauritz, Johan; Jaß, Jana; Milton, Debra L.

doi:10.1099/mic.0.26032-0

Cited by 67 publications

(55 citation statements)

References 49 publications

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“…Related Vibrio species also produce cFP at concentrations similar to that in V. vulnificus, and, furthermore, cFP also enhances the expression of OmpU proteins in these species, suggesting that cFP is a signal molecule common to members of the genus Vibrio. In Vibrio spp., OmpU is implicated in various activities associated with pathogenicity, such as resistance to antimicrobial peptides and bile acids, organic acid tolerance, biofilm formation, attachment to host cells in normal symbiotic relationships, and, possibly, adhesion (1,28,30,40,48,55). Moreover, the expression of OmpU is enhanced by bile and is positively correlated with maximal induction of virulence factors such as cholera toxin and the coregulated pili and with intestinal colonization (39,41).…”

Section: Discussionmentioning

confidence: 99%

Cyclo(Phe-Pro) Modulates the Expression ofompUinVibriospp

et al. 2006

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Vibrio vulnificus was found to produce a chemical that induced the expression of Vibrio fischeri lux genes. Electron spray ionization-mass spectrometry and 1 H nuclear magnetic resonance analyses indicated that the compound was cyclo(L-Phe-L-Pro) (cFP). The compound was produced at a maximal level when cell cultures reached the onset of stationary phase. Sodium dodecyl sulfate-polyacrylamide gel analysis of the total proteins of V. vulnificus indicated that expression of OmpU was enhanced by exogenously added synthetic or purified cFP. A toxR-null mutant failed to express ompU despite the addition of cFP. The related Vibrio spp. V. cholerae, V. parahaemolyticus, and V. harveyi also produced cFP, which induced the expression of their own ompU genes. cFP also enhanced the expression in V. cholerae of the ctx genes, which are known to be regulated by ToxR. Our results suggest that cFP is a signal molecule controlling the expression of genes important for the pathogenicity of Vibrio spp.Communication between cells via diffusible chemicals is a general phenomenon found in virtually all living organisms. However, it is only in the last 2 decades that it has been intensively studied in bacteria. One of the best-known examples is quorum sensing. A number of bacteria associated with eukaryotic hosts employ quorum-sensing systems to sense their population density, thereby modulating the expression of sets of genes involved in physiological responses associated with survival, propagation, and/or virulence (9,21,44). N-Acylhomoserine lactones (AHLs) are the most prevalent signal molecules for quorum sensing in gram-negative bacteria, but not all signal molecules belong to this group. For instance, Vibrio harveyi employs a furanosyl borate diester molecule in addition to AHL (7). The plant pathogen Ralstonia solanacearum uses 3-hydroxypalmitic acid methyl ester together with AHL to control the expression of virulence factors (14), and several gram-positive bacteria utilize peptides or ␥-butyrolactone as signals (for a review, see reference 12). Xanthomonas campestris also uses non-AHL signal molecules, which have been identified as fatty acid derivatives, to regulate the expression of virulence factors (3, 54). In addition, cyclic dipeptides produced by Pseudomonas spp. and some other genera can activate AHL bioindicator strains (22). They probably activate or antagonize signaling components implicated in AHL-dependent quorum sensing by cross talk with the associated sensors. However, the actual biological roles of these cyclic dipeptide molecules remain to be clarified.Vibrio vulnificus is an opportunistic human pathogen that causes severe wound infection and primary septicemia (50). It has been reported to possess a functional luxS and produce a signal molecule that induces bioluminescence in a V. harveyi AI-2 reporter strain (25). It is also known to possess smcR, a homolog of the positive regulatory gene luxR of V. harveyi (29). SmcR induces the expression of vvpE, encoding a metalloprotease, and represses vvhAB, encodin...

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Section: Discussionmentioning

confidence: 99%

Cyclo(Phe-Pro) Modulates the Expression ofompUinVibriospp

et al. 2006

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“…Another gene whose overexpression in the ryhB mutant could negatively influence biofilm formation is ompU. In Vibrio anguillarum, eliminating ompU caused a 10-fold increase in biofilm growth, suggesting that OmpU has an inhibitory effect on biofilm formation (54).…”

Section: Discussionmentioning

confidence: 99%

Characterization of Vibrio cholerae RyhB: the RyhB Regulon and Role of ryhB in Biofilm Formation

2005

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Vibrio cholerae encodes a small RNA with homology to Escherichia coli RyhB. Like E. coli ryhB, V. cholerae ryhB is negatively regulated by iron and Fur and is required for repression of genes encoding the superoxide dismutase SodB and multiple tricarboxylic acid cycle enzymes. However, V. cholerae RyhB is considerably longer (>200 nucleotides) than the E. coli RNA (90 nucleotides), and it regulates the expression of a variety of genes that are not known to be regulated by RyhB in E. coli, including genes involved in motility, chemotaxis, and biofilm formation. A mutant with a deletion in ryhB had reduced chemotactic motility in low-iron medium and was unable to form wild-type biofilms. The defect in biofilm formation was suppressed by growing the mutant in the presence of excess iron or succinate. The wild-type strain showed reduced biofilm formation in iron-deficient medium, further supporting a role for iron in normal biofilm formation. The ryhB mutant was not defective for colonization in a mouse model and appeared to be at a slight advantage when competing with the wild-type parental strain. Other genes whose expression was influenced by RyhB included those encoding the outer membrane porins OmpT and OmpU, several iron transport systems, and proteins containing heme or iron-sulfur clusters. These data indicate that V. cholerae RyhB has diverse functions, ranging from iron homeostasis to the regulation of biofilm formation.Iron plays a critical role in the cellular metabolism of almost all living organisms. Iron is required for processes as diverse as the tricarboxylic acid (TCA) cycle, electron transport, DNA metabolism, and response to oxidative stress. Because iron has the potential for catalyzing production of reactive oxygen species, excess iron can also pose a significant problem. The influx and intracellular fate of iron must therefore be tightly regulated. This is achieved in part through the action of the irondependent negative regulator Fur, which functions to coordinate the iron status of the cell with the expression of genes involved in iron transport, storage, and metabolism. Under iron-replete conditions, Fur complexes with the ferrous ion and blocks transcription of its regulon by binding to conserved regions termed Fur boxes within the promoter region of these genes. There is another layer of complexity in the scheme of iron-and Fur-dependent regulation. In Escherichia coli, certain genes involved in iron storage, iron metabolism, and antioxidant defense appear to be positively regulated by Fur (6,36,42), and this was recently shown to be mediated through the action of a small RNA (sRNA), RyhB (26). RyhB negatively regulates the expression of sodB (encoding superoxide dismutase), ftn and bfr (encoding ferritin and bacterioferritin), and several iron-sulfur cluster-containing TCA cycle enzyme genes, including the sdh operon (encoding succinate dehydrogenase) and acnA (encoding aconitase). Because RyhB is itself negatively regulated by Fur, the net effect is positive regulation of these genes un...

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“…They are basically composed of protein, lipid and sugar, which could be easily recognized as foreign substances by the host's immunological defense systems (Qian et al 2007). These OMPs play an important role in infection and pathogenicity in the host (Tsolis 2002 (Wang et al 2003).…”

Section: Introductionmentioning

confidence: 99%

Immune response in Lutjanus erythropterus induced by the major outer membrane protein (OmpU) of Vibrio alginolyticus

Cai¹,

Yao²,

Lu³

et al. 2010

Dis. Aquat. Org.

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The outer membrane proteins (OMPs) of the marine aquatic animal pathogen Vibrio alginolyticus play an important role in the virulence of the bacterium and are potential candidates for vaccine development. In this study, the major 35.6 kDa OMP of V. alginolyticus was isolated by gel excision from the crude OMP fraction from V. alginolyticus. The sequence of the first 27 amino acid residues from the N-terminal end of the protein is ATV YKD GGT ELL VGG RVE FRG DFI GSD, which has high homology with OmpU proteins from other Vibrio spp. (92%). Lutjanus erythropterus were vaccinated with OmpU, and immunogenicity was confirmed by subsequent western blotting. Enzyme-linked immunosorbent assay (ELISA) analysis demonstrated that OmpU produced an observable antibody response in all sera of the vaccinated fish. L. erythropterus vaccinated with OmpU produced specific antibodies, and were highly resistant to infection with virulent V. alginolyticus. These results indicate that OmpU is an effective vaccine candidate against V. alginolyticus for L. erythropterus. KEY WORDS: Vibrio alginolyticus · Outer membrane protein · OmpU · Immunogenicity · VaccineResale or republication not permitted without written consent of the publisher

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Role for the major outer-membrane protein from Vibrio anguillarum in bile resistance and biofilm formation

Cited by 67 publications

References 49 publications

Cyclo(Phe-Pro) Modulates the Expression ofompUinVibriospp

Cyclo(Phe-Pro) Modulates the Expression ofompUinVibriospp

Characterization of Vibrio cholerae RyhB: the RyhB Regulon and Role of ryhB in Biofilm Formation

Immune response in Lutjanus erythropterus induced by the major outer membrane protein (OmpU) of Vibrio alginolyticus

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