TY  - JOUR
  - Hickey, RM,Twomey, DP,Ross, RP,Hill, C
  - 2003
  - March
  - Microbiology-SGM
  - Production of enterolysin A by a raw milk enterococcal isolate exhibiting multiple virulence factors
  - Validated
  - ()
  - LACTOBACILLUS-CASEI ESCHERICHIA-COLI AGGREGATION SUBSTANCE ANTIBIOTIC-RESISTANCE NUCLEOTIDE-SEQUENCE N-ACETYLMURAMIDASE SURFACE PROTEIN CELL-WALL FAECALIS PLASMID
  - 149
  - 655
  - 664
  - 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.
  - DOI 10.1099/mic.0.25949-0
DA  - 2003/03
ER  - 

@article{V160756090,
   = {Hickey,  RM and Twomey,  DP and Ross,  RP and Hill,  C },
   = {2003},
   = {March},
   = {Microbiology-SGM},
   = {Production of enterolysin A by a raw milk enterococcal isolate exhibiting multiple virulence factors},
   = {Validated},
   = {()},
   = {LACTOBACILLUS-CASEI ESCHERICHIA-COLI AGGREGATION SUBSTANCE ANTIBIOTIC-RESISTANCE NUCLEOTIDE-SEQUENCE N-ACETYLMURAMIDASE SURFACE PROTEIN CELL-WALL FAECALIS PLASMID},
   = {149},
  pages = {655--664},
   = {{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.}},
   = {DOI 10.1099/mic.0.25949-0},
  source = {IRIS}
}