microbiology, Vol 141, 3087-3093, Copyright © 1995 by Society for General Microbiology

ARTICLES

Capnocytophaga gingivalis aminopeptidase: a potential virulence factor

DA Spratt, J Greenman and AG Schaffer
Department of Biological Sciences, Faculty of Applied Sciences, University of the West of England, Bristol, UK.

The production and properties of an aminopeptidase from Capnocytophaga gingivalis were studied. C. gingivalis was grown in continuous culture over a range of dilution rates and the cell-bound and extracellular levels of aminopeptidase and trypsin-like protease (TLPase) measured. At high growth rates (0.6 mu rel) TLPase specific activity was low and found exclusively as cell-bound activity; at low growth rates (0.0375 mu rel), specific activity was high and 26% was found as extracellular activity. In contrast, aminopeptidase specific activity was highest at 0.3 mu rel and the ratio of cell-bound to extracellular activity was relatively constant at all growth rates. Only about 5% of the total activity was extracellular. The aminopeptidase, which has a wide specificity towards artificial substrates, was purified to homogeneity, as judged by SDS-PAGE, from the supernatant fluid of cells grown in continuous culture in a tryptone/glucose/thiamine medium. The enzyme has a molecular mass of 61 kDa, a pl of 6.3, a pH optimum close to 7.5 and showed a requirement for magnesium or calcium ions. The N-terminal sequence of the first 10 amino acids (Asp-Val-Asn-Met-Leu-Trp-Tyr-Val-x- Arg...) showed no similarity to any published sequence. This enzyme in its cell-bound or extracellular form may be important in the nutrition and pathogenesis of C. gingivalis in the human oral cavity.

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