The DOI matches its Crossref record; 68 of the 68 references it cites were found in a registry or an index.
Anchoring of proteins to lactic acid bacteria
Abstract
The anchoring of proteins to the cell surface of lactic acid bacteria (LAB) using genetic techniques is an exciting and emerging research area that holds great promise for a wide variety of biotechnological applications. This paper reviews five different types of anchoring domains that have been explored for their efficiency in attaching hybrid proteins to the cell membrane or cell wall of LAB. The most exploited anchoring regions are those with the LPXTG box that bind the proteins in a covalent way to the cell wall. In recent years, two new modes of cell wall protein anchoring have been studied and these may provide new approaches in surface display. The important progress that is being made with cell surface display of chimaeric proteins in the areas of vaccine development and enzyme- or whole-cell immobilisation is highlighted.
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Fusion of the C-terminal LPXTG containing domain of PrtP with several reporter proteins resulted in the surface exposure of the fusion proteins.
“Fusion of the C-terminal LPXTG containing domain of PrtP with several reporter proteins resulted in the surface exposure of the fusion proteins [28,29].”
From Positive role of cell wall anchored proteinase PrtP in adhesion of lactococci (2007) · cites this paper as [29]
The section on PrtP anchors reports that the Lb. paracasei sorting signal surface-displayed several fused antigens in Lactobacillus species. But it also reports that TTFC fused to the L. lactis PrtP anchor was not detectable on intact cell surfaces and remained in the membrane. The claim therefore overgeneralizes the result across PrtP anchors. (LLM, conf=0.87)
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“Fusion of the C-terminal LPXTG containing domain of PrtP with several reporter proteins resulted in the surface exposure of the fusion proteins [28,29].”
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Metadata
- Authors
- Leenhouts, K., Buist, G., & Kok, J.
- Affiliations
- University of Groningen (NL)
- Corresponding author
- Kok, Jan
- ORCID
- Venue
- Antonie van Leeuwenhoek
- Published
- 1999-11
- Volume
- 76
- Issue
- 1-4
- Pages
- 367-376
- ISSN
- 0003-6072 (ISSN-L)
- 1572-9699
- OpenAlex
- W1832138672
- Cited by
- 97
- References
- 68
- Citations by year
- 2026: 2 · 2025: 2 · 2023: 2 · 2021: 1 · 2020: 1 · 2019: 6 · 2018: 2 · 2017: 3 · 2016: 6 · 2015: 3 · 2014: 8 · 2013: 5 · 2012: 5
- FWCI
- 1.26
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Antonie van Leeuwenhoek (publishedVersion)
- PubMed (publishedVersion)
- University of Groningen research database (University of Groningen / Centre for Information Technology) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Life Sciences › Agricultural and Biological Sciences › Food Science › Probiotics and Fermented Foods
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- lactic acid bacteria, protein anchoring, cell surface display, hybrid proteins, chimaeric proteins, plasma membrane proteins, vaccine development, enzyme immobilization
- MeSH terms
- Bacterial Proteins, Binding Sites, Biotechnology, Cell Membrane, Cell Wall, Gram-Positive Bacteria, Models, Biological, Lactic Acid
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