Antimicrobial psoriasin (S100A7) protects human skin from Escherichia coli infection

Nat Immunol. 2005 Jan;6(1):57-64. doi: 10.1038/ni1142. Epub 2004 Nov 28.

Abstract

Human healthy skin is continuously exposed to bacteria, but is particularly resistant to the common gut bacterium Escherichia coli. We show here that keratinocytes secrete, as the main E. coli-killing compound, the S100 protein psoriasin in vitro and in vivo in a site-dependent way. In vivo treatment of human skin with antibodies to psoriasin inhibited its E. coli-killing properties. Psoriasin was induced in keratinocytes in vitro and in vivo by E. coli, indicating that its focal expression in skin may derive from local microbial induction. Zn(2+)-saturated psoriasin showed diminished antimicrobial activity, suggesting that Zn(2+) sequestration could be a possible antimicrobial mechanism. Thus, psoriasin may be key to the resistance of skin against E. coli.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-Bacterial Agents / pharmacology
  • Anti-Bacterial Agents / therapeutic use*
  • Calcium-Binding Proteins / pharmacology
  • Calcium-Binding Proteins / therapeutic use*
  • Escherichia coli / drug effects*
  • Escherichia coli / metabolism
  • Escherichia coli Infections / prevention & control*
  • Humans
  • Microbial Sensitivity Tests
  • Molecular Sequence Data
  • S100 Calcium Binding Protein A7
  • S100 Proteins
  • Skin / microbiology
  • Zinc / metabolism
  • Zinc / pharmacology

Substances

  • Anti-Bacterial Agents
  • Calcium-Binding Proteins
  • S100 Calcium Binding Protein A7
  • S100 Proteins
  • S100A7 protein, human
  • Zinc

Associated data

  • GENBANK/BC034687
  • GENBANK/M86757
  • RefSeq/NM_002963