Cloning and expression of the damselysin gene from Vibrio damsela

Cutter, David; Kreger, Arnold S.

doi:10.1128/iai.58.1.266-268.1990

Cited by 32 publications

(8 citation statements)

References 25 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…fungi, plants, nematodes and humans). In several cases in which a PLD activity has been identified in prokaryotes, it has been implicated in virulence (Cutter and Kreger, 1990; McNamara et al , 1994; Rudolph et al , 1999). The murine toxin of Y. pestis is a PLD.…”

Section: Discussionmentioning

confidence: 99%

Genetic and biochemical analyses of a eukaryotic‐like phospholipase D of Pseudomonas aeruginosa suggest horizontal acquisition and a role for persistence in a chronic pulmonary infection model

Wilderman

Vasil

Johnson

et al. 2001

Molecular Microbiology

View full text Add to dashboard Cite

Phospholipases D (PLDs) are virtually ubiquitous in eukaryotic organisms; however, they are relatively uncommon in prokaryotes. In this report, we demonstrate that the environmentally acquired, opportunistic pathogen Pseudomonas aeruginosa expresses PLD activity. A gene designated pldA was identified in the genomic database of P. aeruginosa PAO1 encoding a protein with significant homology to eukaryotic PLDs, but not to any prokaryotic PLDs. PldA is most homologous to PLDs from mammals and yeast. The pldA gene was cloned and shown to express an ≈ 116 kDa protein with calcium‐regulated PLD activity that is localized to the periplasm. Interestingly, not all strains of P. aeruginosa carry pldA. When present, pldA is always linked to an open reading frame (ORF), ORF4, and a gene (vgrA1) encoding a protein homologous to Vgr from Escherichia coli. Vgr proteins contain regularly repeated dipeptide motifs (valine‐glycine repeats). In E. coli, genes encoding Vgr are associated with multicopy genetic elements designated Rhs (rearrangement hot‐spots). P. aeruginosa PAO1 has 10 vgr homologues dispersed throughout its genome, but the copy number of these genetic elements varies considerably in different strains. Neither vgrA1 nor ORF4 is present in strains lacking pldA. Furthermore, sequences flanking vgrA1, pldA and ORF4 in the P. aeruginosa strains examined are highly conserved, suggesting a specific site of insertion. These and other data suggest that vgrA1, pldA and ORF4 constitute an ≈ 7 kb mobile genetic element and that pldA was acquired horizontally, perhaps from a eukaryotic organism. Competition studies between a PldA knock‐out mutant and the parental wild‐type strain indicate that PldA contributes to the ability of P. aeruginosa PAO1 to persist in a chronic pulmonary infection model in rats.

show abstract

Section: Discussionmentioning

confidence: 99%

Genetic and biochemical analyses of a eukaryotic‐like phospholipase D of Pseudomonas aeruginosa suggest horizontal acquisition and a role for persistence in a chronic pulmonary infection model

Wilderman

Vasil

Johnson

et al. 2001

Molecular Microbiology

View full text Add to dashboard Cite

show abstract

“…Corynebacterium pseudotuberculosis. Corynebacterium pseudotuberculosis, the agent of caseous lymphadenitis in small ruminants and ulcerative lymphangitis in horses, produces extracellular PLD, which possibly plays a role in the pathogenicity of this and similar bacteria (Corynebacterium ulcerans and Arcanobacterium haemolyticum) (1,34,118,184). The genes encoding the PLD in C. pseudotuberculosis and A. haemolyticum have been cloned and sequenced (118).…”

Section: Bacterial Phospholipasesmentioning

confidence: 99%

Potential Role of Phospholipases in Virulence and Fungal Pathogenesis

2000

View full text Add to dashboard Cite

SUMMARY Microbial pathogens use a number of genetic strategies to invade the host and cause infection. These common themes are found throughout microbial systems. Secretion of enzymes, such as phospholipase, has been proposed as one of these themes that are used by bacteria, parasites, and pathogenic fungi. The role of extracellular phospholipase as a potential virulence factor in pathogenic fungi, including Candida albicans, Cryptococcus neoformans, and Aspergillus, has gained credence recently. In this review, data implicating phospholipase as a virulence factor in C. albicans, Candida glabrata, C. neoformans, and A. fumigatus are presented. A detailed description of the molecular and biochemical approaches used to more definitively delineate the role of phospholipase in the virulence of C. albicans is also covered. These approaches resulted in cloning of three genes encoding candidal phospholipases (caPLP1, caPLB2, and PLD). By using targeted gene disruption, C. albicans null mutants that failed to secrete phospholipase B, encoded by caPLB1, were constructed. When these isogenic strain pairs were tested in two clinically relevant murine models of candidiasis, deletion of caPLB1 was shown to lead to attenuation of candidal virulence. Importantly, immunogold electron microscopy studies showed that C. albicans secretes this enzyme during the infectious process. These data indicate that phospholipase B is essential for candidal virulence. Although the mechanism(s) through which phospholipase modulates fungal virulence is still under investigations, early data suggest that direct host cell damage and lysis are the main mechanisms contributing to fungal virulence. Since the importance of phospholipases in fungal virulence is already known, the next challenge will be to utilize these lytic enzymes as therapeutic and diagnostic targets.

show abstract

“…Phospholipases D are produced by a number of species of pathogenic bacteria, including Corynebacterium utcerans (Abrehem and Zamiri, 1980), Vibrio damseta (Cutter and Kreger, 1990). and Arcanobacterium haemotyticum (Soucek and Souckova, 1964), and may be important virulence factors for these organisms.…”

Section: Goat Challengementioning

confidence: 99%

Targeted mutagenesis of the phospholipase D gene results in decreased virulence ofCorynebacterium pseudotuberculosis

McNamara

Bradley

Songer

1994

Molecular Microbiology

View full text Add to dashboard Cite

The chromosomal gene encoding the phospholipase D from Corynebacterium pseudotuberculosis (biovar ovis) isolate Whetten 1 was replaced with an allele containing a nonsense mutation. The virulence of the mutant strain (W1.31r1) and the isogenic parental strain were then compared by inoculation of goats. The wild-type strain caused abscessation at the site of infection, which then spread to the regional lymph node, while W1.31r1 had a reduced ability to establish a primary infection and was incapable of dissemination. Our results confirm that phospholipase D is a virulence determinant of C. pseudotuberculosis that increases the persistence and spread of the bacteria within the host.

show abstract

Cloning and expression of the damselysin gene from Vibrio damsela

Cited by 32 publications

References 25 publications

Genetic and biochemical analyses of a eukaryotic‐like phospholipase D of Pseudomonas aeruginosa suggest horizontal acquisition and a role for persistence in a chronic pulmonary infection model

Genetic and biochemical analyses of a eukaryotic‐like phospholipase D of Pseudomonas aeruginosa suggest horizontal acquisition and a role for persistence in a chronic pulmonary infection model

Potential Role of Phospholipases in Virulence and Fungal Pathogenesis

Targeted mutagenesis of the phospholipase D gene results in decreased virulence ofCorynebacterium pseudotuberculosis

Contact Info

Product

Resources

About