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    Characterization of acid phosphatase activities in the equine pathogen Streptococcus equi

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    Publication date
    2000-10
    Author
    Hamilton, A.
    Harrington, Dean J.
    Sutcliffe, I.C.
    Keyword
    Acid phosphatase; Lipoprotein; Streptococcus; Strangles
    Peer-Reviewed
    Yes
    
    Metadata
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    Abstract
    Acid phosphatases hydrolyse phosphomonoesters at acidic pH in a variety of physiological contexts. The recently defined class C family of acid phosphatases includes the 32 kDa LppC lipoprotein of Streptococcus equisimilis. To define further the distribution of acid phosphatases in the genus Streptococcus we have examined the equine pathogens Streptococcus equi subsp. equi and Streptococcus equi subsp. zooepidemicus. Whole cell assays indicated that these organisms possess two acid phosphatases with activity optima at pH 5.0 and pH 6.0-6.5 and that only the former of these was, like LppC, resistant to EDTA. Western blotting with a polyclonal anti-LppC antiserum revealed the presence of a cross-reactive 32 kDa protein in both organisms. The cross-reactive protein in S. equi was shown to be a surface accessible lipoprotein as its processing was inhibited by the antibiotic globomycin and it was released from whole cells by treatment with trypsin. The presence of DNA sequences homologous to the S. equisimilis lppC gene were confirmed by PCR. These data strongly suggest that Streptococcus equi subsp. equi and Streptococcus equi subsp. zooepidemicus produce a lipoprotein acid phosphatase homologous to LppC of S. equisimilis.
    URI
    http://hdl.handle.net/10454/11590
    Version
    No full-text in the repository
    Citation
    Hamilton A, Harrington DJ and Sutcliffe IC (2000) Characterization of acid phosphatase activities in the equine pathogen Streptococcus equi. Systematic and Applied Microbiology. 23(3): 325-329.
    Link to publisher’s version
    http://dx.doi.org/10.1016/S0723-2020(00)80060-0
    Type
    Article
    Collections
    Life Sciences Publications

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