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Cited by 83Bacterial biofilms and quorum sensingProtease and Inhibitor MechanismsEnzyme Production and Characterization

Inhibition of human lymphocyte proliferation and cleavage of interleukin-2 by Pseudomonas aeruginosa proteases

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Theander, T G, Kharazmi, A, Pedersen, B K, Christensen, L D, Tvede, N, Poulsen, L K, Odum, N, Svenson, M, Bendtzen, K·1988·Infection and Immunity
DOI 10.1128/iai.56.7.1673-1677.1988PMC PMC259461
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Abstract

This study was undertaken to determine the effect of Pseudomonas aeruginosa alkaline protease (AP) and elastase (ELA) on human lymphocyte function. AP at 50 micrograms/ml and ELA at 12 micrograms/ml caused a 50% inhibition of phytohemagglutinin-induced proliferation. There was no difference in the effect of proteases on CD4- and CD8-positive cells. To determine the effect of proteases on interleukin-2 (IL-2)-induced cell proliferation, the proteases and IL-2 were added to the IL-2-dependent CTLL-2 cell line. AP and ELA inhibited the proliferation of these cells. When IL-2 was added in excess, the inhibition was partly reversed. ELA at 10 micrograms/ml cleaved IL-2, as judged by size chromatography of a reaction mixture containing 125I-labeled IL-2 and the proteases. The ELA-digested IL-2 exhibited a reduced binding capacity to IL-2 receptors on the lymphocytes. Furthermore, treatment of phytohemagglutinin-stimulated lymphocytes with AP and ELA resulted in inhibition of binding of intact IL-2 to IL-2 receptors on the stimulated lymphocytes. These results indicated that P. aeruginosa-derived enzymes are able to interfere with human lymphocyte function in vitro and that this effect might be due to cleavage of IL-2.

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Crossref · 10.1128/iai.56.7.1673-1677.1988

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  • Alkaline proteases and elastase from Pseudomonas aeruginosa can degrade IL-2 and interferon (INF)-γ.

    “Previous reports have shown that alkaline proteases and elastase from Pseudomonas aeruginosa can degrade IL-2 and interferon (INF)-γ.146,147”

    From The emerging roles of bacterial proteases in intestinal diseases (2023) · cites this paper as [147]

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Authors
Theander, T. G., Kharazmi, A., Pedersen, B. K., Christensen, L. D., Tvede, N., Poulsen, L. K., Odum, N., Svenson, M., & Bendtzen, K.
Affiliations
  • Rigshospitalet (DK)
  • Department of Infectious Diseases, Rigshospitalet, Copenhagen, Denmark.
ORCID
Venue
Infection and Immunity
Publisher
American Society for Microbiology
Published
1988-07
Volume
56
Issue
7
Pages
1673-1677
ISSN
  • 0019-9567 (ISSN-L)
  • 1098-5522
DOI
10.1128/iai.56.7.1673-1677.1988
PMC
PMC259461
OpenAlex
W1526462522
Cited by
83
References
35
Citations by year
2026: 2 · 2025: 2 · 2024: 4 · 2023: 2 · 2021: 6 · 2020: 4 · 2019: 2 · 2018: 1 · 2017: 2 · 2016: 2 · 2015: 3 · 2014: 5 · 2012: 1
FWCI
1.85
Type
journal article
Language
en
Open access
Licence
journals.asm.org/non-commercial-tdm-license (tdm)
Locations
  • Infection and Immunity (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
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 › Biotechnology › Enzyme Production and Characterization
Keywords
Pseudomonas aeruginosa, alkaline protease, elastase, interleukin-2, proteolytic cleavage, lymphocyte proliferation, phytohemagglutinin, CTLL-2 cells, CD4 and CD8 T cells, bacterial virulence factors
MeSH terms
Binding, Competitive, Humans, Immunosuppressive Agents, Interleukin-2, Lymphocyte Activation, Lymphocytes, Pancreatic Elastase, Endopeptidases, Phytohemagglutinins, Pseudomonas aeruginosa, Receptors, Immunologic, Serine Endopeptidases, Receptors, Interleukin-2

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