Psoriasin, a novel anti-Candida albicans adhesin

J Mol Med (Berl). 2018 Jun;96(6):537-545. doi: 10.1007/s00109-018-1637-6. Epub 2018 May 7.

Abstract

Candida albicans belongs to the normal microbial flora on epithelial surfaces of humans. However, under certain, still not fully understood conditions, it can become pathogenic and cause a spectrum of diseases, from local infections to life-threatening septicemia. We investigated a panel of antimicrobial proteins and peptides (AMPs), potentially involved in mucosal immunity against this pathogen. Out of six studied AMPs, psoriasin was most up-regulated during a mucosal infection, an acute episode of recurrent Candida vulvovaginitis, although candidacidal activity has not been demonstrated. We here show that psoriasin binds to β-glucan, a basic component of the C. albicans cell wall, and thereby inhibits adhesion of the pathogen to surfaces and increases IL-8 production by mucosal epithelial cells. In conclusion, we show a novel mechanism of action of psoriasin. By inhibiting C. albicans adhesion and by enhancing cytokine production, psoriasin contributes to the immune response against C. albicans. KEY MESSAGES: The antimicrobial peptide psoriasin is highly up-regulated during a local mucosal infection, Candida albicans vulvovaginitis. Psoriasin binds to β-glucan in the Candida albicans cell wall and thereby inhibits adhesion of the pathogen. Binding of psoriasin to Candida albicans induces an immune response by mucosal epithelial cells.

Keywords: Adhesion; Candida albicans; Immune response; Psoriasin; β-Glucan.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adult
  • Candida albicans / physiology
  • Candidiasis / genetics
  • Candidiasis / metabolism*
  • Cell Adhesion
  • Cell Line
  • Female
  • Humans
  • S100 Calcium Binding Protein A7 / genetics
  • S100 Calcium Binding Protein A7 / metabolism*
  • Young Adult
  • beta-Glucans / metabolism

Substances

  • S100 Calcium Binding Protein A7
  • S100A7 protein, human
  • beta-Glucans