ArticleApplied and environmental microbiology2011
Identification of candidate carrier proteins for surface display on Lactococcus lactis by theoretical and experimental analyses of the surface proteome.
Article in Applied and environmental microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 40 citations in OpenAlex.
- Secretome Profiling ofAntibiotics (Basel, Switzerland) · 2026Article
- Incorporation of recombinant proteins into extracellular vesicles by Lactococcus cremoris.Scientific reports · 2025Article
- Roles of Mature Domain Targeting Signals (MTSs) for Protein Translocation and Secretion inInternational journal of molecular sciences · 2024Article
- Aerobic adaptation and metabolic dynamics ofmSystems · 2024Article
- Double-Labeling Method for Visualization and Quantification of Membrane-Associated Proteins inInternational journal of molecular sciences · 2023Article
- Development of a Novel Cell Surface Attachment System to Display Multi-Protein Complex Using the Cohesin-Dockerin Binding Pair.Journal of microbiology and biotechnology · 2021Article
- Another Breaker of the Wall: the Biological Function of the Usp45 Protein of Lactococcus lactis.Applied and environmental microbiology · 2020Article
- Engineering recombinant Lactococcus lactis as a delivery vehicle for BPC-157 peptide with antioxidant activities.Applied microbiology and biotechnology · 2018Article
- A review on Lactococcus lactis: from food to factory.Microbial cell factories · 2017Review
- Article
- Adhesion of the genome-sequenced Lactococcus lactis subsp. cremoris IBB477 strain is mediated by specific molecular determinants.Applied microbiology and biotechnology · 2016Article
- Display of recombinant proteins at the surface of lactic acid bacteria: strategies and applications.Microbial cell factories · 2016Review
- Development of Recombinant Lactococcus lactis Displaying Albumin-Binding Domain Variants against Shiga Toxin 1 B Subunit.PloS one · 2016Article
- Characterizing the surface-exposed proteome of Planococcus halocryophilus during cryophilic growth.Extremophiles : life under extreme conditions · 2015Article
- Lactic acid bacteria--20 years exploring their potential as live vectors for mucosal vaccination.Applied microbiology and biotechnology · 2015Review
- Surface proteome analysis of a natural isolate of Lactococcus lactis reveals the presence of pili able to bind human intestinal epithelial cells.Molecular & cellular proteomics : MCP · 2013Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lactococcus lactis is a lactic acid bacterium of proven safety for use in human oral applications. For this purpose, surface display of recombinant proteins is important, and new approaches for it are being sought. Analysis of the bacterial surface proteome is essential in identifying new candidate carrier proteins for surface display. We have made two different predictions of surface-associated proteins of L. lactis MG1363 by using Augur and LocateP software, which yielded 666 and 648 proteins, respectively. Surface proteins of L. lactis NZ9000, a derivative of MG1363, were identified by using a proteomics approach. The surface proteins were cleaved from intact bacteria, and the resulting peptides were identified by mass spectrometry. The latter approach yielded 80 proteins, 34 of which were not predicted by either software. Of the 80 proteins, 7 were selected for further study. These were cloned in frame with a C-terminal hexahistidine tag and overexpressed in L. lactis NZ9000 using nisin-controlled expression. Proteins of correct molecular weight carrying a hexahistidine tag were detected. Their surface localization was confirmed with flow cytometry. Basic membrane protein A (BmpA) was exposed at the highest level. To test BmpA as a candidate carrier protein, the hexahistidine tag was replaced by the B domain of staphylococcal protein A in the genetic construct. The B domain was displayed on the surface with BmpA as a carrier. The advantage of covalent BmpA binding was demonstrated. BmpA was thus shown to be a suitable candidate for a carrier protein in lactococcal surface display.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.