Comparative Structure Analysis of the Multi-Domain, Cell Envelope Proteases of Lactic Acid Bacteria
Open accessPreprint — published as 10.3390/microorganisms11092256 · Paper page
Abstract
Lactic acid bacteria (LAB) have an extracellular proteolytic system that includes a multi-domain, cell envelope protease (CEP) with a subtilisin homologous protease domain. These CEPs have different proteolytic activities despite having similar protein sequences. Structural characterization has previously been limited to CEP homologs of dairy and human derived LAB strains, excluding CEPs of plant derived LAB strains. CEP structures are a challenge to determine experimentally due to their large size and attachment to the cell envelope. This study aims to clarify the prevalence and structural diversity of CEPs by using the structure prediction software AlphaFold 2. Domain boundaries are clarified based on a comparative analysis of 21 three-dimensional structures, revealing novel domain architectures of CEP homologs that are not necessarily restricted to specific LAB species or ecological niches. The C-terminal flanking region of the protease domain is divided into fibronectin type-III-like domains with various structural traits. The analysis also emphasizes the existence of two distinct domains for cell envelope attachment that are preceded by an intrinsically disordered cell wall spanning domain. The domain variants and their combinations provide CEPs with different stability, proteolytic activity and potentially adhesive properties, making CEPs targets for steering proteolytic activity with relevance for both food development and human health.
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Cites
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764 · see citing works
Positive role of cell wall anchored proteinase PrtP in adhesion of lactococci
Habimana, O., Le Goff, C., Juillard, V., Bellon-Fontaine, M.-N., Buist, G., Kulakauskas, S., & Briandet, R. (2007) · BMC Microbiology · doi:10.1186/1471-2180-7-36 · Cited by 58 · see citing works
Modeled Structure of the Cell Envelope Proteinase of Lactococcus lactis
Hansen, E. B., & Marcatili, P. (2020) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2020.613986 · Cited by 16 · see citing works
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Neviani, E., Levante, A., & Gatti, M. (2024) · Fermentation · doi:10.3390/fermentation10040186 · Cited by 17 · see citing works
- Authors
- Christensen, L. F., Høie, M. H., Bang-Berthelsen, C. H., Marcatili, P., & Hansen, E. B.
- Affiliations
- Technical University of Denmark (DK)
- Corresponding author
- Christensen, Lise Friis
- Hansen, Egon Bech
- Venue
- Microorganisms
- Publisher
- MDPI AG
- Published
- 2023-08-04
- Volume
- 11
- Issue
- 9
- Pages
- 2256-2256
- ISSN
- 2076-2607 (ISSN-L)
- PMC
- PMC10535647
- OpenAlex
- W4386560814
- Cited by
- 17
- References
- 3
- Citations by year
- 2026: 4 · 2025: 4 · 2024: 8 · 2023: 1
- FWCI
- 2.45
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Microorganisms (publishedVersion, cc-by)
- Preprints.org (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Technical University of Denmark, DTU Orbit (Technical University of Denmark, DTU) (submittedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Innovationsfonden (7045-00021B)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Food Science › Probiotics and Fermented Foods
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Keywords
- lactic acid bacteria, subtilisin-like protease, protein structure prediction, AlphaFold2, intrinsically disordered regions, domain architecture, extracellular proteolysis, proteolytic activity
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