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Title: A fibronectin receptor on Candida albicans mediates adherence of the fungus to extracellular matrix

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 bloodborne fungi by providing for adherence of the microorganisms to ECM proteins.

Authors:
;  [1]
  1. (Overton Brooks VA Medical Center, Shreveport, LA (USA))
Publication Date:
OSTI Identifier:
6061466
Resource Type:
Journal Article
Journal Name:
Journal of Infectious Diseases; (USA)
Additional Journal Information:
Journal Volume: 163:3; Journal ID: ISSN 0022-1899
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; CANDIDA; ADHESION; FUNGAL DISEASES; PATHOGENESIS; PROTEINS; RECEPTORS; BIOCHEMICAL REACTION KINETICS; IODINE 125; BETA DECAY RADIOISOTOPES; DAYS LIVING RADIOISOTOPES; DISEASES; ELECTRON CAPTURE RADIOISOTOPES; EUMYCOTA; FUNGI; INFECTIOUS DISEASES; INTERMEDIATE MASS NUCLEI; IODINE ISOTOPES; ISOTOPES; KINETICS; MEMBRANE PROTEINS; MICROORGANISMS; NUCLEI; ODD-EVEN NUCLEI; ORGANIC COMPOUNDS; PLANTS; RADIOISOTOPES; REACTION KINETICS; YEASTS; 550201* - Biochemistry- Tracer Techniques; 550901 - Pathology- Tracer Techniques

Citation Formats

Klotz, S.A., and Smith, R.L. A fibronectin receptor on Candida albicans mediates adherence of the fungus to extracellular matrix. United States: N. p., 1991. Web. doi:10.1093/infdis/163.3.604.
Klotz, S.A., & Smith, R.L. A fibronectin receptor on Candida albicans mediates adherence of the fungus to extracellular matrix. United States. doi:10.1093/infdis/163.3.604.
Klotz, S.A., and Smith, R.L. Fri . "A fibronectin receptor on Candida albicans mediates adherence of the fungus to extracellular matrix". United States. doi:10.1093/infdis/163.3.604.
@article{osti_6061466,
title = {A fibronectin receptor on Candida albicans mediates adherence of the fungus to extracellular matrix},
author = {Klotz, S.A. and Smith, R.L.},
abstractNote = {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 bloodborne fungi by providing for adherence of the microorganisms to ECM proteins.},
doi = {10.1093/infdis/163.3.604},
journal = {Journal of Infectious Diseases; (USA)},
issn = {0022-1899},
number = ,
volume = 163:3,
place = {United States},
year = {1991},
month = {3}
}