Source:http://linkedlifedata.com/resource/pubmed/id/12634334
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 3
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pubmed:dateCreated |
2003-3-13
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pubmed:databankReference | |
pubmed:abstractText |
Even though enterococci are a common cause of human infection they can readily be isolated from a range of food sources, including various meat and dairy products. An enterococcal strain, DPC5280, which exhibits a broad spectrum of inhibition against many Gram-positive bacteria was recently isolated from an Irish raw milk sample. Characterization of the inhibition revealed that the strain exhibits haemolytic activity characteristic of the two-component lantibiotic cytolysin and also produces a heat-labile antimicrobial protein of 34 kDa. The latter protein displayed cell wall hydrolytic activity, as evidenced by zymogram gels containing autoclaved lactococcal cells. N-terminal sequencing of the purified protein yielded the sequence ASNEWS which is 100 % identical to enterolysin A (accession no. AF249740), a protein which shares 28 and 29 % identity to the Gly-Gly endopeptidases, lysostaphin and zoocin A, respectively. Indeed, amplification of entL from DPC5280 and sequencing revealed that the protein is 100 % identical to enterolysin A. The DPC5280 strain also contained the determinants associated with multiple virulence factors, including gelatinase, aggregation substance and multiple antibiotic resistance. The linkage of this cell-wall-degrading enzyme to other virulence factors in enterococci may contribute to the competitiveness of pathogenic enterococci when found in complex microbial environments such as food and the gastrointestinal tract.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Bacteriocins,
http://linkedlifedata.com/resource/pubmed/chemical/Cytotoxins,
http://linkedlifedata.com/resource/pubmed/chemical/Virulence Factors,
http://linkedlifedata.com/resource/pubmed/chemical/cytolysin, Enterococcus faecalis
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1350-0872
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
149
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
655-64
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12634334-Amino Acid Sequence,
pubmed-meshheading:12634334-Animals,
pubmed-meshheading:12634334-Bacterial Proteins,
pubmed-meshheading:12634334-Bacteriocins,
pubmed-meshheading:12634334-Base Sequence,
pubmed-meshheading:12634334-Cell Wall,
pubmed-meshheading:12634334-Cytotoxins,
pubmed-meshheading:12634334-Enterococcus faecalis,
pubmed-meshheading:12634334-Gram-Positive Bacteria,
pubmed-meshheading:12634334-Hemolysis,
pubmed-meshheading:12634334-Milk,
pubmed-meshheading:12634334-Molecular Sequence Data,
pubmed-meshheading:12634334-Virulence,
pubmed-meshheading:12634334-Virulence Factors
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pubmed:year |
2003
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pubmed:articleTitle |
Production of enterolysin A by a raw milk enterococcal isolate exhibiting multiple virulence factors.
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pubmed:affiliation |
Teagasc, Dairy Products Research Centre, Moorepark, Fermoy, Co Cork, Ireland.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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