Escherichia coli outer membrane protein A adheres to human brain microvascular endothelial cells

Sooan Shin, Gengshi Lu, Mian Cai, Kwang Sik Kim

Research output: Contribution to journalArticlepeer-review

Abstract

Escherichia coli K1 is the most common gram-negative bacterium causing neonatal meningitis. The outer membrane protein A (OmpA) assembles a β-barrel structure having four surface-exposed loops in E. coli outer membrane. OmpA of meningitis-causing E. coli K1 is shown to contribute to invasion of the human brain microvascular endothelial cells (HBMEC), the main cellular component of the blood-brain barrier (BBB). However, the direct evidence of OmpA protein interacting with HBMEC is not clear. In this study, we showed that OmpA protein, solubilized from the outer membrane of E. coli, adhered to HBMEC surface. To verify OmpA interaction with the HBMEC, we purified N-terminal membrane-anchoring β-barrel domain of OmpA and all surface-exposed loops deleted OmpA proteins, and showed that the surface-exposed loops of OmpA were responsible for adherence to HBMEC. These findings indicate that the OmpA is the adhesion molecule with HBMEC and the surface-exposed loops of OmpA are the determinant of this interaction.

Original languageEnglish (US)
Pages (from-to)1199-1204
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume330
Issue number4
DOIs
StatePublished - May 20 2005

Keywords

  • Bacterial adhesin
  • Human brain endothelial cell
  • Meningitis
  • Outer membrane protein
  • β-barrel domain

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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