Open AccessHuman brain endothelial ATP synthase β‐subunit is mannose‐insensitive binding target of FimH
Author(s) -
Shin Sooan,
Kim Kwang Sik
Publication year - 2010
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2009.01878.x
Subject(s) - mannose , protein subunit , atp synthase , biology , microbiology and biotechnology , biochemistry , enzyme , gene
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 β‐subunit and actin proteins from the surface biotinylated HBMEC as the mannose‐insensitive binding targets for FimH. Co‐immunoprecipitation experiments in the presence of α‐methyl mannose verified the binding of FimH to ATP synthase β‐subunit of HBMEC. ATP synthase β‐subunit antibody decreased E. coli K1 binding to HBMEC in the presence of α‐methyl mannose. Taken together, these findings demonstrate that FimH of E. coli K1 binds to HBMEC in both mannose‐sensitive and ‐insensitive manner.