A fibronectin receptor on candida albicans mediates adherence of the fungus to extracellular matrix

Stephen A. Klots, Robert L. Smith

Research output: Contribution to journalArticle

90 Scopus citations

Abstract

Binding of fibronectin, an extracellular matrix (ECM) protein, to Candida albicans was measured, and adherence of the fungus to immobilized ECM proteins, fibronectin, laminin, types I and IV collagen, and subendothelial ECM was studied.125I-labeled fibronectin was inhibited from binding to the fungus by unlabeled human plasma fibronectin and by Arg-Gly-Asp (RGD), Gly-Arg-Gly-Glu-Ser-Pro (GRGESP), and Gly-Arg-Gly-Asp-Thr-Pro (GRGDTP), but binding was not inhibited by Gly-Arg-Gly-Asp-Ser-Pro. Soluble fibronectin, RGD, GRGESP, and GRGDTP also inhibited fungal adherence to the individual immobilized ECM proteins in a complex pattern, but only soluble fibronectin (10-7 M) inhibited fungal adherence to subendothelial ECM. Thus, C. albicans possesses at least one type of cell surface receptor for binding soluble fibronectin that can be inhibited with peptides. This receptor apparently is used to bind the fungus to immobilized ECM proteins and to subendothelial ECM and may play a role in the initiation of disseminated disease by bloodbome fungi by providing for adherence of the microorganisms to ECM proteins.

Original languageEnglish (US)
Pages (from-to)604-610
Number of pages7
JournalJournal of Infectious Diseases
Volume163
Issue number3
DOIs
StatePublished - Mar 1991
Externally publishedYes

ASJC Scopus subject areas

  • Immunology and Allergy
  • Infectious Diseases

Fingerprint Dive into the research topics of 'A fibronectin receptor on candida albicans mediates adherence of the fungus to extracellular matrix'. Together they form a unique fingerprint.

  • Cite this