TY - JOUR
T1 - Hemoglobin differentially induces binding of Candida, Trichosporon, and Saccharomyces species to fibronectin
AU - Rodrigues, Rui G.
AU - Yan, Sizhuang
AU - Walsh, Thomas J.
AU - Roberts, David D.
N1 - Copyright:
Copyright 2017 Elsevier B.V., All rights reserved.
PY - 1998
Y1 - 1998
N2 - Fibronectin (FN) is an abundant host protein that is specifically recognized by several pathogenic yeasts. Binding of FN in solution to Candida, Trichosporon, and Saccharomyces species is increased 20- to 110- fold by growth in medium containing hemoglobin, but specific adhesion to immobilized FN is increased only in Candida albicans, Candida tropicalis, Candida krusei, and Candida glabrata. Hemoglobin induces both specific and nonspecific binding of soluble FN. Nonspecific binding accounts for all of the enhancement in Trichosporon beigelii and Saccharomyces cerevisiae, but the Candida species possess a saturable, high-affinity binding site for FN that is induced by hemoglobin. Induction of displaceable soluble FN binding correlates with the ability of hemoglobin to regulate adhesion to immobilized FN, since hemoglobin does not induce adhesion of S. cerevisiae or T. beigelii to immobilized FN. Regulation by hemoglobin of FN binding to Candida species may therefore be an important factor in the pathogenesis in these yeast infections.
AB - Fibronectin (FN) is an abundant host protein that is specifically recognized by several pathogenic yeasts. Binding of FN in solution to Candida, Trichosporon, and Saccharomyces species is increased 20- to 110- fold by growth in medium containing hemoglobin, but specific adhesion to immobilized FN is increased only in Candida albicans, Candida tropicalis, Candida krusei, and Candida glabrata. Hemoglobin induces both specific and nonspecific binding of soluble FN. Nonspecific binding accounts for all of the enhancement in Trichosporon beigelii and Saccharomyces cerevisiae, but the Candida species possess a saturable, high-affinity binding site for FN that is induced by hemoglobin. Induction of displaceable soluble FN binding correlates with the ability of hemoglobin to regulate adhesion to immobilized FN, since hemoglobin does not induce adhesion of S. cerevisiae or T. beigelii to immobilized FN. Regulation by hemoglobin of FN binding to Candida species may therefore be an important factor in the pathogenesis in these yeast infections.
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U2 - 10.1086/515639
DO - 10.1086/515639
M3 - Article
C2 - 9697732
AN - SCOPUS:0031821824
VL - 178
SP - 497
EP - 502
JO - Journal of Infectious Diseases
JF - Journal of Infectious Diseases
SN - 0022-1899
IS - 2
ER -