PROPERTIES OF PROTEINASE FROM<i>STREPTOCOCCUS FAECALIS</i>VAR.<i>LIQUEFACIENS</i>

Bleiweis, Arnold S.; Zimmerman, Leonard N.

doi:10.1128/jb.88.3.653-659.1964

Cited by 40 publications

(7 citation statements)

References 12 publications

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“…Hynes reported that the inhibitory activity of hematin increased as pH levels of the assay medium decreased [21]. Enterococcal protease has been previously reported to be a metalloendopeptidase, sensitive to EDTA [22,23] and our present findings are consistent with this.…”

Section: Discussionsupporting

confidence: 92%

Inhibition of mutans streptococci by the hematin formed on blood-containing media by proteolytic enterococci

James

Tagg

1987

FEMS Microbiology Letters

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Section: Discussionsupporting

confidence: 92%

Inhibition of mutans streptococci by the hematin formed on blood-containing media by proteolytic enterococci

James

Tagg

1987

FEMS Microbiology Letters

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“…Purification of a 28-to 32-kDa metalloproteinase from E. faecalis was first described 30 years ago (19). In 1989 Makinen et al (153) published a description of the substrate specificity of protease produced by E. faecalis OG1-10, a human oral isolate.…”

Section: Cytolysinmentioning

confidence: 99%

Virulence of enterococci

1994

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Enterococci are commensal organisms well suited to survival in intestinal and vaginal tracts and the oral cavity. However, as for most bacteria described as causing human disease, enterococci also possess properties that can be ascribed roles in pathogenesis. The natural ability of enterococci to readily acquire, accumulate, and share extrachromosomal elements encoding virulence traits or antibiotic resistance genes lends advantages to their survival under unusual environmental stresses and in part explains their increasing importance as nosocomial pathogens. This review discusses the current understanding of enterococcal virulence relating to (i) adherence to host tissues, (ii) invasion and abscess formation, (iii) factors potentially relevant to modulation of host inflammatory responses, and (iv) potentially toxic secreted products. Aggregation substance, surface carbohydrates, or fibronectin-binding moieties may facilitate adherence to host tissues. Enterococcus faecalis appears to have the capacity to translocate across intact intestinal mucosa in models of antibiotic-induced superinfection. Extracellular toxins such as cytolysin can induce tissue damage as shown in an endophthalmitis model, increase mortality in combination with aggregation substance in an endocarditis model, and cause systemic toxicity in a murine peritonitis model. Finally, lipoteichoic acid, superoxide production, or pheromones and corresponding peptide inhibitors each may modulate local inflammatory reactions.

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“…fragments as a consequence of the protease activity (4,200). S. faecalis, frequently identified as the etiological agent of various opportunistic infections, produces an extracellular zinc-containing metalloprotease (19,31). This enzyme was recently further characterized biochemically and had a similar substrate specificity to that of thermolysin (147).…”

Section: Staphylococcus Sppmentioning

confidence: 99%