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

FEMS Microbiol Lett. 2007 Aug;273(1):1-11. doi: 10.1111/j.1574-6968.2007.00778.x. Epub 2007 Jun 6.

Abstract

The OmpA outer membrane protein of Escherichia coli and other enterobacteria is a multifaceted protein. This protein is expressed to very high levels and ompA is tightly regulated at the posttranscriptional level. It can function as an adhesin and invasin, participate in biofilm formation, act as both an immune target and evasin, and serves as a receptor for several bacteriophages. Many of these properties are due to four short protein loops that emanate from the protein to the outside of the cell. Herein it is described how the structure of this protein relates to its many functions.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Bacterial Outer Membrane Proteins / chemistry*
  • Bacterial Outer Membrane Proteins / genetics
  • Bacterial Outer Membrane Proteins / immunology
  • Bacterial Outer Membrane Proteins / physiology*
  • Escherichia coli / chemistry*
  • Escherichia coli / physiology*
  • Escherichia coli Proteins / chemistry*
  • Escherichia coli Proteins / genetics
  • Escherichia coli Proteins / immunology
  • Escherichia coli Proteins / physiology*
  • Gene Expression Regulation, Bacterial
  • Models, Molecular
  • Molecular Sequence Data

Substances

  • Bacterial Outer Membrane Proteins
  • Escherichia coli Proteins
  • OMPA outer membrane proteins