Susceptibility of Staphylococcus aureus bacteremia strains to different skin-derived antimicrobial proteins

Arch Dermatol Res. 2012 Oct;304(8):633-7. doi: 10.1007/s00403-012-1284-7. Epub 2012 Sep 6.

Abstract

Staphylococcus aureus is a major human pathogen causing cutaneous infections to life-threatening bacteremia. These infections are often caused by strains derived from the own microflora suggesting that a disturbed epidermal barrier may promote invasion of S. aureus. Antimicrobial peptides and proteins (AMP) such as human beta-defensin-3 and RNase 7 contribute to control the colonization of S. aureus on the skin surface. This leads to the hypothesis that strains with a decreased susceptibility toward skin-derived AMP may better overcome the innate cutaneous defence barrier increasing the possibility of invading into the blood stream. To address this hypothesis we determined whether S. aureus strains from bacteremia patients are less susceptible to various skin-derived AMP than strains from healthy carriers. No differences in the AMP-killing activity against bacteremia-derived S. aureus and control strains were detected suggesting that the onset of S. aureus bacteremia is not based on the varying susceptibilities against skin-derived AMP.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adolescent
  • Adult
  • Aged
  • Antimicrobial Cationic Peptides / immunology*
  • Antimicrobial Cationic Peptides / pharmacology
  • Apoptosis / genetics
  • Bacteremia / immunology
  • Bacteremia / microbiology
  • Drug Resistance, Bacterial
  • Female
  • Humans
  • Male
  • Microbial Sensitivity Tests
  • Middle Aged
  • Ribonucleases / immunology*
  • Ribonucleases / pharmacology
  • Skin / immunology*
  • Skin / microbiology
  • Species Specificity
  • Staphylococcal Infections / immunology*
  • Staphylococcus aureus / drug effects*
  • Staphylococcus aureus / genetics
  • Staphylococcus aureus / pathogenicity
  • Young Adult
  • beta-Defensins / immunology*
  • beta-Defensins / pharmacology

Substances

  • Antimicrobial Cationic Peptides
  • DEFB103A protein, human
  • beta-Defensins
  • Ribonucleases
  • Ribonuclease 7