Degradation of outer membrane protein A in Escherichia coli killing by neutrophil elastase

Science. 2000 Aug 18;289(5482):1185-8. doi: 10.1126/science.289.5482.1185.

Abstract

In determining the mechanism of neutrophil elastase (NE)-mediated killing of Escherichia coli, we found that NE degraded outer membrane protein A (OmpA), localized on the surface of Gram-negative bacteria. NE killed wild-type, but not OmpA-deficient, E. coli. Also, whereas NE-deficient mice had impaired survival in response to E. coli sepsis, as compared to wild-type mice, the presence or absence of NE had no influence on survival in response to sepsis that had been induced with OmpA-deficient E. coli. These findings define a mechanism of nonoxidative bacterial killing by NE and point to OmpA as a bacterial target in host defense.

Publication types

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

MeSH terms

  • Animals
  • Bacterial Outer Membrane Proteins / genetics
  • Bacterial Outer Membrane Proteins / metabolism*
  • Blood Bactericidal Activity*
  • Cell Membrane / metabolism
  • Cell Membrane / ultrastructure
  • Colony Count, Microbial
  • Escherichia coli / genetics
  • Escherichia coli / growth & development
  • Escherichia coli / metabolism*
  • Escherichia coli / ultrastructure
  • Escherichia coli Infections / immunology
  • Escherichia coli Infections / microbiology
  • Humans
  • Leukocyte Elastase / antagonists & inhibitors
  • Leukocyte Elastase / genetics
  • Leukocyte Elastase / metabolism*
  • Mice
  • Microscopy, Electron
  • Mutation
  • Neutrophils / enzymology*
  • Neutrophils / microbiology
  • Phagosomes / enzymology
  • Phagosomes / microbiology
  • Proteinase Inhibitory Proteins, Secretory
  • Proteins / pharmacology
  • Serine Proteinase Inhibitors / pharmacology

Substances

  • Bacterial Outer Membrane Proteins
  • Proteinase Inhibitory Proteins, Secretory
  • Proteins
  • Serine Proteinase Inhibitors
  • OMPA outer membrane proteins
  • Leukocyte Elastase