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Cited by 161Bacterial Genetics and BiotechnologyHeat shock proteins researchProtease and Inhibitor Mechanisms

The DOI matches its Crossref record; 146 of the 146 references it cites were found in a registry or an index.

Bacterial Proteases and Virulence

Frees, Dorte, Brøndsted, Lone, Ingmer, Hanne·2013·Subcellular Biochemistry
DOI 10.1007/978-94-007-5940-4_7
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Abstract

Bacterial pathogens rely on proteolysis for variety of purposes during the infection process. In the cytosol, the main proteolytic players are the conserved Clp and Lon proteases that directly contribute to virulence through the timely degradation of virulence regulators and indirectly by providing tolerance to adverse conditions such as those experienced in the host. In the membrane, HtrA performs similar functions whereas the extracellular proteases, in close contact with host components, pave the way for spreading infections by degrading host matrix components or interfering with host cell signalling to short-circuit host cell processes. Common to both intra- and extracellular proteases is the tight control of their proteolytic activities. In general, substrate recognition by the intracellular proteases is highly selective which is, in part, attributed to the chaperone activity associated with the proteases either encoded within the same polypeptide or on separate subunits. In contrast, substrate recognition by extracellular proteases is less selective and therefore these enzymes are generally expressed as zymogens to prevent premature proteolytic activity that would be detrimental to the cell. These extracellular proteases are activated in complex cascades involving auto-processing and proteolytic maturation. Thus, proteolysis has been adopted by bacterial pathogens at multiple levels to ensure the success of the pathogen in contact with the human host.

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Crossref · 10.1007/978-94-007-5940-4_7

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Research works printed but not linked: 4

  1. Molière N, Turgay K (2013) General and regulatory proteolysis in Bacillus subtilis. In: Dougan DA (ed) Regulated proteolysis in microorganisms. Springer, Subcell Biochem 66:3–33
  2. Gur E (2013) The Lon AAA+ protease. In: Dougan DA (ed) Regulated proteolysis in microorganisms. Springer, Subcell Biochem 66:35–51
  3. Champion OL, Karlyshev AV, Senior NJ, Woodward M et al (2010) Insect infection model for Campylobacter jejuni reveals that O-methyl phosphoramidate has insecticidal activity. J Infect Dis 201(5):776–782
  4. Arvidson S (2006) Extracellular enzymes. In: Fischetti VA (ed) Gram-positive pathogens (2nd edn.). ASM Press.

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Metadata

Authors
Frees, D., Brøndsted, L., & Ingmer, H.
Affiliations
University of Copenhagen (DK)
Corresponding author
Ingmer, Hanne
ORCID
Venue
Subcellular Biochemistry
Publisher
Springer Netherlands
Published
2013
Volume
66
Pages
161-192
ISSN
0306-0225 (ISSN-L)
DOI
10.1007/978-94-007-5940-4_7
OpenAlex
W155982093
Cited by
159
References
146
Citations by year
2026: 5 · 2025: 9 · 2024: 5 · 2023: 15 · 2022: 11 · 2021: 12 · 2020: 37 · 2019: 13 · 2018: 11 · 2017: 15 · 2016: 6 · 2015: 7 · 2014: 7 · 2013: 6
FWCI
22.02
Type
book chapter
Language
en
Open access
closed
Licence
Locations
  • Sub-cellular biochemistry/Subcellular biochemistry (publishedVersion)
  • PubMed (publishedVersion)
  • Research at the University of Copenhagen (University of Copenhagen) (submittedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
Keywords
bacterial proteases, bacterial virulence, Clp protease, Lon protease, HtrA protease, extracellular protease, stress tolerance, substrate specificity, chaperone activity, zymogen activation, proteolytic maturation, host cell signalling, bacterial pathogenesis
MeSH terms
Bacteria, Bacterial Proteins, Humans, Peptide Hydrolases, Virulence, Signal Transduction, Molecular Chaperones, Proteolysis

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