Human brain endothelial ATP synthase β-subunit is mannose-insensitive binding target of FimH

Sooan Shin, Kwang Sik Kim

Research output: Contribution to journalArticle

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 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.

Original languageEnglish (US)
Pages (from-to)156-162
Number of pages7
JournalFEMS Microbiology Letters
Volume303
Issue number2
DOIs
StatePublished - Feb 2010

Fingerprint

Mannose
Endothelial Cells
Adenosine Triphosphate
Brain
Escherichia coli Meningitis
Escherichia coli
Protein Subunits
Blood-Brain Barrier
Immunoprecipitation
Actins
Membrane Proteins
Antibodies

Keywords

  • ATP synthase β-subunit
  • FimH
  • HBMEC

ASJC Scopus subject areas

  • Microbiology
  • Genetics
  • Molecular Biology

Cite this

Human brain endothelial ATP synthase β-subunit is mannose-insensitive binding target of FimH. / Shin, Sooan; Kim, Kwang Sik.

In: FEMS Microbiology Letters, Vol. 303, No. 2, 02.2010, p. 156-162.

Research output: Contribution to journalArticle

@article{2ade86b573d34069bda69d6d5f8da19d,
title = "Human brain endothelial ATP synthase β-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 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.",
keywords = "ATP synthase β-subunit, FimH, HBMEC",
author = "Sooan Shin and Kim, {Kwang Sik}",
year = "2010",
month = "2",
doi = "10.1111/j.1574-6968.2009.01878.x",
language = "English (US)",
volume = "303",
pages = "156--162",
journal = "FEMS Microbiology Letters",
issn = "0378-1097",
publisher = "Wiley-Blackwell",
number = "2",

}

TY - JOUR

T1 - Human brain endothelial ATP synthase β-subunit is mannose-insensitive binding target of FimH

AU - Shin, Sooan

AU - Kim, Kwang Sik

PY - 2010/2

Y1 - 2010/2

N2 - 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.

AB - 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.

KW - ATP synthase β-subunit

KW - FimH

KW - HBMEC

UR - http://www.scopus.com/inward/record.url?scp=75149121104&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=75149121104&partnerID=8YFLogxK

U2 - 10.1111/j.1574-6968.2009.01878.x

DO - 10.1111/j.1574-6968.2009.01878.x

M3 - Article

C2 - 20067530

AN - SCOPUS:75149121104

VL - 303

SP - 156

EP - 162

JO - FEMS Microbiology Letters

JF - FEMS Microbiology Letters

SN - 0378-1097

IS - 2

ER -