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

Abstract:

:Escherichia coli K1 is the most common gram-negative bacterium causing neonatal meningitis. The outer membrane protein A (OmpA) assembles a beta-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 beta-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.

authors

Shin S,Lu G,Cai M,Kim KS

doi

10.1016/j.bbrc.2005.03.097

subject

Has Abstract

pub_date

2005-05-20 00:00:00

pages

1199-204

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(05)00604-2

journal_volume

330

pub_type

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