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Analyzing the Permeability of the Blood-Brain Barrier by Microbial Traversal through Microvascular Endothelial Cells
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Escherichia coli outer membrane protein A adheres to human brain microvascular endothelial cells

Sooan Shin1, Gengshi Lu, Mian Cai

  • 1Division of Infectious Diseases, Department of Pediatrics, Johns Hopkins University School of Medicine, Baltimore, MD 21287, USA.

Biochemical and Biophysical Research Communications
|April 13, 2005
PubMed

Insights

Escherichia coli K1 outer membrane protein A (OmpA) adheres to human brain cells. Surface-exposed loops of OmpA mediate this interaction, identifying it as a key adhesion molecule in neonatal meningitis.

Area of Science:

  • Microbiology
  • Cell Biology
  • Immunology

Background:

  • Escherichia coli K1 is a leading cause of Gram-negative neonatal meningitis.
  • The outer membrane protein A (OmpA) in E. coli K1 is implicated in crossing the blood-brain barrier (BBB).
  • Direct evidence for OmpA's interaction with human brain microvascular endothelial cells (HBMEC) is lacking.

Purpose of the Study:

  • To investigate the direct interaction between E. coli K1 OmpA and HBMEC.
  • To identify the specific domains of OmpA responsible for HBMEC adherence.

Main Methods:

  • Solubilization of OmpA from E. coli outer membranes.
  • Purification of the N-terminal beta-barrel domain of OmpA.
  • Generation of OmpA variants with deleted surface-exposed loops.
  • Assessment of OmpA and its variants' adherence to HBMEC.

Main Results:

  • Solubilized OmpA protein from E. coli directly adhered to the surface of HBMEC.
  • OmpA variants lacking surface-exposed loops showed significantly reduced adherence to HBMEC.
  • The surface-exposed loops of OmpA were identified as the critical determinants for HBMEC interaction.

Conclusions:

  • OmpA functions as an adhesion molecule mediating the interaction between E. coli K1 and HBMEC.
  • The surface-exposed loops of OmpA are crucial for its binding to the cells of the blood-brain barrier.
  • These findings provide direct evidence for OmpA's role in the pathogenesis of E. coli K1 meningitis.

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