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