title: Human brain endothelial ATP synthase beta-subunit is mannose-insensitive binding target of FimH.
abstract: Binding of meningitis-causing Escherichia coli K1 to human brain microvascular endothelial cells (HBMEC) contributes to traversal of the blood-brain barrier, which occurs in part by the mannose-sensitive binding of FimH. In this study, we showed that FimH also binds to HBMEC, independent of mannose, and identified ATP synthase beta-subunit and actin proteins from the surface biotinylated HBMEC as the mannose-insensitive binding targets for FimH. Co-immunoprecipitation experiments in the presence of alpha-methyl mannose verified the binding of FimH to ATP synthase beta-subunit of HBMEC. ATP synthase beta-subunit antibody decreased E. coli K1 binding to HBMEC in the presence of alpha-methyl mannose. Taken together, these findings demonstrate that FimH of E. coli K1 binds to HBMEC in both mannose-sensitive and -insensitive manner.
authors.affiliation: Division of Pediatric Infectious Diseases, Johns Hopkins University School of Medicine, Baltimore, MD 21287, USA.
authors.forename: Sooan
authors.initials: S
authors.lastname: Shin
authors.forename: Kwang Sik
authors.initials: KS
authors.lastname: Kim
mesh_terms: D018830:Adhesins, Escherichia coli / Q000378:metabolism*; D001921:Brain / Q000382:microbiology; D002478:Cells, Cultured; D042783:Endothelial Cells / Q000201:enzymology* / Q000382:microbiology; D004926:Escherichia coli / Q000472:pathogenicity*; D036781:Fimbriae Proteins / Q000378:metabolism*; D006801:Humans; D047468:Immunoprecipitation; D008358:Mannose / Q000378:metabolism*; D025261:Mitochondrial Proton-Translocating ATPases / Q000378:metabolism*; D011485:Protein Binding
chemical_list: C506526:ATP5F1B protein, human; D018830:Adhesins, Escherichia coli; C058769:fimH protein, E coli; D036781:Fimbriae Proteins; D025261:Mitochondrial Proton-Translocating ATPases; D008358:Mannose