{"database":"biostudies-literature","file_versions":[],"scores":{"citationCount":0,"reanalysisCount":0,"viewCount":48,"searchCount":0},"additional":{"submitter":["Shin S"],"funding":["NIAID NIH HHS","NINDS NIH HHS"],"pagination":["156-62"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2864485"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["303(2)"],"pubmed_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."],"journal":["FEMS microbiology letters"],"pubmed_title":["Human brain endothelial ATP synthase beta-subunit is mannose-insensitive binding target of FimH."],"pmcid":["PMC2864485"],"funding_grant_id":["R01 AI047225","R01 AI047225-05","NS 26310","R01 NS026310","R01 NS026310-21","AI 47225","R56 NS026310"],"pubmed_authors":["Shin S","Kim KS"],"view_count":["48"],"additional_accession":[]},"is_claimable":false,"name":"Human brain endothelial ATP synthase beta-subunit is mannose-insensitive binding target of FimH.","description":"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.","dates":{"release":"2010-01-01T00:00:00Z","publication":"2010 Feb","modification":"2024-12-04T03:09:03.963Z","creation":"2019-03-27T00:30:34Z"},"accession":"S-EPMC2864485","cross_references":{"pubmed":["20067530"],"doi":["10.1111/j.1574-6968.2009.01878.x"]}}