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Cited by 363Neutrophil, Myeloperoxidase and Oxidative MechanismsAntimicrobial Peptides and ActivitiesProtease and Inhibitor Mechanisms

The DOI matches its Crossref record; 15 of the 15 references it cites were found in a registry or an index.

Degradation of Outer Membrane Protein A in Escherichia coli Killing by Neutrophil Elastase

Belaaouaj, Abderr azzaq, Kim, Kwang Sik, Shapiro, Steven D.·2000·Science
DOI 10.1126/science.289.5482.1185
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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.

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Crossref · 10.1126/science.289.5482.1185

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15 of 15 references verified0 citation errors · 0 not checkable

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Citations

Cites

Research works printed but not linked: 3

  1. J. Blondin A. Janoff J. C. Powers in Neutral Proteases of Human Polymorphonuclear Leukocytes J. Havemann and A. Janoff Eds. (Urban and Schwartzenberg Baltimore MD 1978) pp. 39–55.
  2. Beesley J. E., Day S. E., Betts M. P., Thorley C. M., J. Gen. Microbiol. 130, 1481 (1984).
  3. We thank J. Gaither-Ganim J. Campbell and M. Veith for their excellent technical support R. M. Senior and M. Caparon for critical review of the manuscript and A. A. Todorov for statistical analysis. All of the animal experiments were in accordance with Washington University Animal Studies Committee guidelines. This work was supported by a Barnes-Jewish Hospital foundation grant (to A.B.) and by the NIH (to S.D.S. and K.S.K.).

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Metadata

Authors
Belaaouaj, A. A., Kim, K. S., & Shapiro, S. D.
Affiliations
  • Washington University in St. Louis (US)
  • Children's Hospital Los Angeles (US)
Corresponding author
Belaaouaj, Abderr azzaq
ORCID
Venue
Science
Publisher
American Association for the Advancement of Science (AAAS)
Published
2000-08-18
Volume
289
Issue
5482
Pages
1185-1187
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
DOI
10.1126/science.289.5482.1185
OpenAlex
W2027297714
Cited by
363
References
15
Citations by year
2026: 7 · 2025: 10 · 2024: 9 · 2023: 10 · 2022: 11 · 2021: 15 · 2020: 15 · 2019: 20 · 2018: 24 · 2017: 12 · 2016: 13 · 2015: 16 · 2014: 15 · 2013: 17 · 2012: 15
FWCI
4.95
Type
journal article
Language
en
Open access
closed
Locations
  • Science (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
  • Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
Keywords
neutrophil elastase, OmpA, Escherichia coli, neutrophil killing, Gram-negative bacteria, sepsis, host defense, bacterial surface proteins
MeSH terms
Animals, Bacterial Outer Membrane Proteins, Blood Bactericidal Activity, Cell Membrane, Escherichia coli, Escherichia coli Infections, Humans, Microscopy, Electron, Mutation, Neutrophils, Phagosomes, Proteins, Colony Count, Microbial, Serine Proteinase Inhibitors, Leukocyte Elastase, Mice, Proteinase Inhibitory Proteins, Secretory

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