TY - JOUR
T1 - Binding characteristics of S fimbriated Escherichia coli to isolated brain microvascular endothelial cells
AU - Stins, Monique F.
AU - Prasadarao, Nemani V.
AU - Ibric, Luminita
AU - Wass, Carol A.
AU - Luckett, Peter
AU - Kim, Kwang Sik
N1 - Copyright:
Copyright 2005 Elsevier B.V., All rights reserved.
PY - 1994/11
Y1 - 1994/11
N2 - To assess the role of S fimbriae in the pathogenesis of Escherichia coli meningitis, transformants of E. coli strains with or without S fimbriae plasmid were compared for their binding to microvessel endothelial cells isolated from bovine brain cortices (BMEC). The BMEC's displayed a cobblestone appearance, were positive for factor VIII, carbonic anhydrase IV, took up fluorescent-labeled acetylated low density lipoprotein, and exhibited gamma glutamyl transpeptidase activity. Binding of S fimbriated E. coli to BMEC was approximately threefold greater than nonfimbriated E. coli Similarly S fimbriated E. coli bound to human brain endothelial cells approximately threefold greater than nonfimbriated E. coli Binding was reduced approximately 60% by isolated S fimbriae and about 80% by anti-S adhesin antibody. Mutating the S adhesin gene resulted in a complete loss of the binding, whereas mutagenesis of the major S fimbriae subunit gene sfaA did not significantly affect binding. Pretreatment of BMEC with neuraminidase or prior incubation of S fimbriated E. coli with NeuAcα2,3-sialyl lactose completely abolished binding. These findings indicate that S fimbriated E. coli bind to NeuAcα2,3-galactose containing glycoproteins on brain endothelial cells via a lectin-like activity of SfaS adhesin. This might be an important early step in the penetration of bacteria across the blood- brain barrier in the development of E. coli meningitis.
AB - To assess the role of S fimbriae in the pathogenesis of Escherichia coli meningitis, transformants of E. coli strains with or without S fimbriae plasmid were compared for their binding to microvessel endothelial cells isolated from bovine brain cortices (BMEC). The BMEC's displayed a cobblestone appearance, were positive for factor VIII, carbonic anhydrase IV, took up fluorescent-labeled acetylated low density lipoprotein, and exhibited gamma glutamyl transpeptidase activity. Binding of S fimbriated E. coli to BMEC was approximately threefold greater than nonfimbriated E. coli Similarly S fimbriated E. coli bound to human brain endothelial cells approximately threefold greater than nonfimbriated E. coli Binding was reduced approximately 60% by isolated S fimbriae and about 80% by anti-S adhesin antibody. Mutating the S adhesin gene resulted in a complete loss of the binding, whereas mutagenesis of the major S fimbriae subunit gene sfaA did not significantly affect binding. Pretreatment of BMEC with neuraminidase or prior incubation of S fimbriated E. coli with NeuAcα2,3-sialyl lactose completely abolished binding. These findings indicate that S fimbriated E. coli bind to NeuAcα2,3-galactose containing glycoproteins on brain endothelial cells via a lectin-like activity of SfaS adhesin. This might be an important early step in the penetration of bacteria across the blood- brain barrier in the development of E. coli meningitis.
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M3 - Article
C2 - 7977653
AN - SCOPUS:0028099213
SN - 0002-9440
VL - 145
SP - 1228
EP - 1236
JO - American Journal of Pathology
JF - American Journal of Pathology
IS - 5
ER -