Virulence of Enterococcus isolates collected in Lower Silesia (Poland)

Scand J Infect Dis. 2005;37(9):630-6. doi: 10.1080/00365540510031421.

Abstract

148 enterococcal strains: E.faecalis (108), E.faecium (35), E.gallinarum (3), E.casseliflavus (1) and E.durans (1) from various clinical specimens were investigated for their ability to adhere to Caco-2 and HEp-2 cell lines, and also for the presence of the esp gene, biofilm formation, production of haemolysins, DNAse and lipase. Several types of enterococcal adhesion to both cell lines were noted. An aggregative adherence was the most frequent among E.faecalis and E.faecium isolates. Other species presented various adhesive types. The occurrence of virulence factors in the whole group of strains was as follows: esp gene in 53.4%, biofilm in 45.3%, haemolysins in 15.5%, DNAse in 12.2% and lipase in 33.1% of enterococcal isolates. It appears that the adherence of the enterococci studied was not significantly associated with the presence of virulence factors.

MeSH terms

  • Bacterial Adhesion
  • Bacterial Proteins / genetics
  • Biofilms / growth & development
  • Caco-2 Cells
  • Cell Line
  • Deoxyribonucleases / metabolism
  • Enterococcus / classification
  • Enterococcus / genetics
  • Enterococcus / isolation & purification
  • Enterococcus / pathogenicity*
  • Enterococcus faecalis / classification
  • Enterococcus faecalis / genetics
  • Enterococcus faecalis / isolation & purification
  • Enterococcus faecalis / pathogenicity
  • Enterococcus faecium / classification
  • Enterococcus faecium / genetics
  • Enterococcus faecium / isolation & purification
  • Enterococcus faecium / pathogenicity
  • Gram-Positive Bacterial Infections / microbiology*
  • Gram-Positive Bacterial Infections / physiopathology
  • Hemolysin Proteins / metabolism
  • Humans
  • Lipase / metabolism
  • Membrane Proteins / genetics
  • Poland
  • Polymerase Chain Reaction
  • Virulence

Substances

  • Bacterial Proteins
  • Hemolysin Proteins
  • Membrane Proteins
  • enterococcal surface protein, esp
  • Deoxyribonucleases
  • Lipase