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A molecular Swiss army knife: OmpA structure, function and expression.

Stephen G J Smith1, Vivienne Mahon, Matthew A Lambert

  • 1Department of Clinical Microbiology, Trinity College Dublin, St James's Hospital, Dublin, Ireland. sgsmith@tcd.ie

FEMS Microbiology Letters
|June 15, 2007
PubMed
Summary
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The outer membrane protein A (OmpA) in E. coli has many roles, including adhesion and acting as a phage receptor. Its structure, particularly its outer loops, dictates these diverse functions.

Area of Science:

  • Microbiology
  • Structural Biology
  • Bacteriology

Background:

  • The OmpA protein is abundant in the outer membrane of E. coli and other enterobacteria.
  • OmpA exhibits diverse functions, including adhesion, invasion, biofilm formation, immune evasion, and bacteriophage receptor activity.
  • Its functions are significantly influenced by structural features, particularly external loops.

Purpose of the Study:

  • To elucidate the relationship between the structure of the OmpA protein and its multifaceted functions.
  • To highlight the role of the protein's external loops in mediating its various biological activities.

Main Methods:

  • Structural analysis of the OmpA protein.
  • Correlation of structural features with known functional data.

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Main Results:

  • The OmpA protein's structure, especially its four external loops, is critical for its diverse roles.
  • These structural elements enable OmpA to function as an adhesin, invasin, and immune modulator.
  • The loops also facilitate OmpA's role as a receptor for bacteriophages.

Conclusions:

  • The structure-function relationship of OmpA is key to understanding its importance in bacterial physiology and pathogenesis.
  • Targeting OmpA's structural loops could offer strategies for combating bacterial infections.