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Cited by 181Bacterial biofilms and quorum sensingProtease and Inhibitor MechanismsBacterial Genetics and Biotechnology

Proteolytic inactivation of cytokines by Pseudomonas aeruginosa

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Parmely, M, Gale, A, Clabaugh, M, Horvat, R, Zhou, W W·1990·Infection and Immunity
DOI 10.1128/iai.58.9.3009-3014.1990PMC PMC313603
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Abstract

Pseudomonas aeruginosa alkaline protease and elastase are thought to contribute to bacterial invasiveness, tissue damage, and immune suppression in animals and patients infected with the bacterium. This study examined the ability of the two proteases to inactivate a number of cytokines that mediate immune and inflammatory responses. Human recombinant gamma interferon (rIFN-gamma) and human recombinant tumor necrosis factor alpha were inactivated by both proteases. Murine rIFN-gamma was relatively resistant to alkaline protease but was inactivated by elastase, and human recombinant interleukin-1 alpha and recombinant interleukin-1 beta were resistant to the effects of both proteases. Western immunoblots suggested that cytokine inactivation by these proteases, where it occurred, required only limited proteolysis of the polypeptides. The ability of different P. aeruginosa strains to inactivate IFN-gamma appeared to require the production of both proteases for optimum activity. These results indicate that in vitro cytokine inactivation by Pseudomonas proteases is selective, requires only limited proteolysis, and in certain instances reflects the cooperative effects of both proteases.

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  1. Dinarello C. A. Interleukin-1. Rev Infect Dis. 1984 Jan-Feb;6(1):51–95. doi: 10.1093/clinids/6.1.51. [DOI] [PubMed] [Google Scholar] · DOI

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Authors
Parmely, M., Gale, A., Clabaugh, M., Horvat, R., & Zhou, W. W.
Affiliations
University of Kansas Medical Center (US)
ORCID
Gale, A
Venue
Infection and Immunity
Publisher
American Society for Microbiology
Published
1990-09
Volume
58
Issue
9
Pages
3009-3014
ISSN
  • 0019-9567 (ISSN-L)
  • 1098-5522
DOI
10.1128/iai.58.9.3009-3014.1990
PMC
PMC313603
OpenAlex
W2100693319
Cited by
181
References
40
Citations by year
2026: 4 · 2025: 5 · 2024: 5 · 2023: 3 · 2022: 6 · 2021: 10 · 2020: 6 · 2019: 12 · 2018: 5 · 2017: 4 · 2016: 3 · 2015: 6 · 2014: 7 · 2013: 7 · 2012: 7
FWCI
1.43
Type
journal article
Language
en
Open access
Licence
journals.asm.org/non-commercial-tdm-license (tdm)
Locations
  • Infection and Immunity (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Institutes of Health (5r01ai023337-03, 2s07rr005373-31)
  • National Institute of Allergy and Infectious Diseases (AI23337)
  • National Center for Research Resources (RR 05373)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bacterial biofilms and quorum sensing
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Keywords
Pseudomonas aeruginosa, alkaline protease, elastase, interferon-gamma, TNF-α, interleukin-1, limited proteolysis, immunosuppression, bacterial virulence
MeSH terms
Animals, Bacterial Proteins, Biological Factors, Humans, Interferon-gamma, Interleukin-1, Metalloendopeptidases, Protein Denaturation, Pseudomonas aeruginosa, Recombinant Proteins, Serine Endopeptidases, Tumor Necrosis Factor-alpha, Cytokines, Mice

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