Microbial metalloproteases and pathogenesis

Miyoshi, Shin Ichi; Shinoda, Sumió

doi:10.1016/s1286-4579(00)00280-x

Cited by 306 publications

(301 citation statements)

References 49 publications

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“…It should be noted that one of 8 these cleavage sites is identical with that of plasma kallikrein (Hovinga et al, 1994). On the studies using synthetic oligopeptide substrates, as well as other bacterial metalloproteases of the thermolysin family (Morihara and Tsuzuki, 1971), V. vulnificus metalloprotease have been believed to hydrolyze specifically the peptide bond at the amino group side of the P 1 ' amino acid residue, usually a hydrophobic amino acid residue (Miyoshi and Shinoda, 2000). The results shown in the present study using the native protein substrates are apparently consistent with this conclusion.…”

Section: Activation and Fragmentation Of Human Zymogens By V Vulnifisupporting

confidence: 86%

“…This human pathogen secretes a zinc metalloprotease of the thermolysin family (Hooper, 1994;Miyoshi and Shinoda, 2000) as an important virulence determinant (Miyoshi and Shinoda, 1993). For instance, when injected into the dorsal skin of a guinea pig, V. vulnificus metalloprotease enhances vascular permeability through activation of the factor XII-plasma kallikrein-kinin cascade that results in liberation of bradykinin, an inflammatory mediator, from high-molecular-weight kininogen (Miyoshi et al, 1987;Molla et al, 1989).…”

Section: Introductionmentioning

confidence: 99%

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Generation of active fragments from human zymogens in the brady kinin-generating cascade by extracellular proteases from Vibrio vulnificus and V. parahaemolyticus

Miyoshi

Watanabe

Kawase

et al. 2004

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Vibrio vulnificus is an opportunistic human pathogen causing septicemia, and the infection is characterized by formation of the edematous skin lesions on limbs. This pathogenic species secretes a thermolysin-like metalloprotease as a virulence determinant. The metalloprotease was confirmed to activate human factor XII-plasma kallikrein-kinin cascade that results in liberation of bradykinin, a chemical mediator enhancing the vascular permeability, from high-molecular weight kininogen. Namely, the metalloprotease showed to generate active fragments by cleavage of Arg-Ile, Arg-Val or Gly-Leu peptide bond in human zymogens (plasma prekallikrein and factor XII). In spite of induction of the sufficient vascular permeability-enhancing and edema-forming reaction in the guinea pig model, a serine protease from V. parahaemolyticus, a human pathogen causing primarily watery diarrhea, showed far less ability to activate and to cleave the human zymogens. These results in part may explain why only V. vulnificus often causes serious edematous skin damages in humans.

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Section: Activation and Fragmentation Of Human Zymogens By V Vulnifisupporting

confidence: 86%

Section: Introductionmentioning

confidence: 99%

Generation of active fragments from human zymogens in the brady kinin-generating cascade by extracellular proteases from Vibrio vulnificus and V. parahaemolyticus

Miyoshi

Watanabe

Kawase

et al. 2004

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“…Proteases, especially metalloproteases, contribute to virulence in pathogenic bacteria including P. aeruginosa, S. marcescens and B. thuringiensis [66][67][68] . In addition to degrading AMPs, proteases might be involved in the destruction of cells and tissues to facilitate colonization of the insect body 69 .…”

Section: Box 3 | Heritable Microorganismsmentioning

confidence: 99%

Bacterial strategies to overcome insect defences

2008

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| Recent genetic and molecular analyses have revealed how several strategies enable bacteria to persist and overcome insect immune defences. Genetic and genomic tools that can be used with Drosophila melanogaster have enabled the characterization of the pathways that are used by insects to detect bacterial invaders and combat infection. Conservation of bacterial virulence factors and insect immune repertoires indicates that there are common strategies of host invasion and pathogen eradication. Long-term interactions of bacteria with insects might ensure efficient dissemination of pathogens to other hosts, including humans. R E V I E W S302 | APRIL 2008 | voLUME 6 www.nature.com/reviews/micro

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“…These four genes are located at synteny break points between the genomes of P. entomophila and other Pseudomonas spp. PSEEN1550 is the homolog of the alkaline protease AprA, which has been shown to be involved in various virulence processes among different species 18 . AprA likely plays a key role in virulence because pathogenicity is affected in mutants defective in PrtR, the predicted transcriptional regulator of aprA (see below).…”

Section: Toxins Against Insectsmentioning

confidence: 99%

Complete genome sequence of the entomopathogenic and metabolically versatile soil bacterium Pseudomonas entomophila

et al. 2006

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Pseudomonas entomophila is an entomopathogenic bacterium that, upon ingestion, kills Drosophila melanogaster as well as insects from different orders. The complete sequence of the 5.9-Mb genome was determined and compared to the sequenced genomes of four Pseudomonas species. P. entomophila possesses most of the catabolic genes of the closely related strain P. putida KT2440, revealing its metabolically versatile properties and its soil lifestyle. Several features that probably contribute to its entomopathogenic properties were disclosed. Unexpectedly for an animal pathogen, P. entomophila is devoid of a type III secretion system and associated toxins but rather relies on a number of potential virulence factors such as insecticidal toxins, proteases, putative hemolysins, hydrogen cyanide and novel secondary metabolites to infect and kill insects. Genome-wide random mutagenesis revealed the major role of the two-component system GacS/GacA that regulates most of the potential virulence factors identified.

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Microbial metalloproteases and pathogenesis

Cited by 306 publications

References 49 publications

Generation of active fragments from human zymogens in the brady kinin-generating cascade by extracellular proteases from Vibrio vulnificus and V. parahaemolyticus

Generation of active fragments from human zymogens in the brady kinin-generating cascade by extracellular proteases from Vibrio vulnificus and V. parahaemolyticus

Bacterial strategies to overcome insect defences

Complete genome sequence of the entomopathogenic and metabolically versatile soil bacterium Pseudomonas entomophila

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