Autolysis of Lactococcus lactis Is Influenced by Proteolysis
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The autolysin AcmA of Lactococcus lactis was shown to be degraded by the extracellular lactococcal proteinase PrtP. Autolysis, as evidenced by reduction in optical density of a stationary-phase culture and concomitant release of intracellular proteins, was greatly reduced when L. lactis MG1363 cells expressed the cell wall-anchored lactococcal proteinase PrtP of the PI-type caseinolytic specificity (PI). On the other hand, lactococcal strains that did not produce the proteinase showed a high level of autolysis, which was also observed when the cells produced the secreted form of PI or a cell wall-anchored proteinase with PIII-type specificity. Autolysis was also increased when MG1363 expressed the cell wall-anchored hybrid PI/PIII-type proteinase PIac. Zymographic analysis of AcmA activity during stationary phase showed that AcmA was quickly degraded by PI and much more slowly by PrtP proteinases with PIII-type and intermediate specificities. Autolysis of L. lactis by AcmA was influenced by the specificity, amount, and location of the lactococcal proteinase. No autolysis was observed when the various proteinases were expressed in an L. lactis acmA deletion mutant, indicating that PrtP itself did not cause lysis of cells. The chain length of a strain was significantly shortened when the strain expressed a cell wall-anchored active proteinase.
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The higher affinity of inactive PRTP* could be explained by degradation of the main lactococcal autolysin AcmA by PRTP+.
“This effect could be explained by degradation of main lactococcal autolysin AcmA by PRTP+ [39].”
From Positive role of cell wall anchored proteinase PrtP in adhesion of lactococci (2007) · cites this paper as [39]
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“This effect could be explained by degradation of main lactococcal autolysin AcmA by PRTP+ [39].”
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Kok, J., & Buist, G. (2003) · Springer eBooks · doi:10.1007/978-1-4615-7090-5_7 · Cited by 2 · see citing works
Self-citationBroadbent, J. R., & Steele, J. L. (2012) · Handbook of Proteolytic Enzymes · doi:10.1016/b978-0-12-382219-2.00837-1 · Cited by 2 · see citing works
Clinical development of lactocepin: a novel bacterial biologic?
Huynegem, K. V., & Steidler, L. (2012) · Expert Review of Clinical Immunology · doi:10.1586/eci.12.55 · Cited by 1 · see citing works
Price, C. E., dos Santos, F. B., Hesseling, A., Uusitalo, J. J., Bachmann, H., Benavente, V., Goel, A., Berkhout, J., Bruggeman, F. J., Marrink, . J., et al. (2017) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/147926 · Cited by 1 · see citing works
Self-citation
- Authors
- Buist, G., Venema, G., & Kok, J.
- Affiliations
- University of Groningen (NL)
- ORCID
- Venue
- Journal of Bacteriology
- Publisher
- American Society for Microbiology
- Published
- 1998-11-15
- Volume
- 180
- Issue
- 22
- Pages
- 5947-5953
- ISSN
- 0021-9193 (ISSN-L)
- 1098-5530
- PMC
- PMC107669
- OpenAlex
- W2144240368
- Cited by
- 68
- References
- 40
- Citations by year
- 2025: 1 · 2023: 2 · 2021: 2 · 2020: 1 · 2019: 1 · 2017: 3 · 2016: 2 · 2015: 2 · 2014: 2 · 2013: 1 · 2012: 4
- FWCI
- 2.47
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Bacteriology (publishedVersion)
- PubMed Central (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed (publishedVersion)
- University of Groningen research database (University of Groningen / Centre for Information Technology) (publishedVersion, other-oa)
- University of Groningen research database (University of Groningen / Centre for Information Technology) (submittedVersion, other-oa)
- Funders
- Koninklijke Nederlandse Akademie van Wetenschappen
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Agricultural and Biological Sciences › Food Science › Probiotics and Fermented Foods
- Physical Sciences › Environmental Science › Ecology › Bacteriophages and microbial interactions
- Keywords
- Lactococcus lactis, autolysis, proteolysis, stationary phase, intracellular protein release
- MeSH terms
- Bacteriolysis, Muramidase, Serine Endopeptidases, Lactococcus lactis
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