ArticleThe Journal of biological chemistry2014
Defining the structure and receptor binding domain of the leaderless bacteriocin LsbB.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 38 citations in OpenAlex.
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- Flow cytometric detection of vancomycin-resistant Enterococcus faecium in urine using fluorescently labelled enterocin K1.Scientific reports · 2023Article
- The role of site-2-proteases in bacteria: a review on physiology, virulence, and therapeutic potential.microLife · 2023Review
- Bacteriocins Revitalize Non-Effective Penicillin G to Overcome Methicillin-ResistantAntibiotics (Basel, Switzerland) · 2022Article
- Exploring the Therapeutic Potenital of the Leaderless Enterocins K1 and EJ97 in the Treatment of Vancomycin-Resistant Enterococcal Infection.Frontiers in microbiology · 2021Article
- Use of Fecal Slurry Cultures to Study In Vitro Effects of Bacteriocins on the Gut Bacterial Populations of Infants.Probiotics and antimicrobial proteins · 2020Article
- The Increasing Issue of Vancomycin-Resistant Enterococci and the Bacteriocin Solution.Probiotics and antimicrobial proteins · 2020Review
- Multifunctional Acidocin 4356 CombatsApplied and environmental microbiology · 2020Article
- Genetic and Biochemical Evidence ThatFrontiers in microbiology · 2019Article
- Lactococcin B Is Inactivated by Intrinsic Proteinase PrtP Digestion inFrontiers in microbiology · 2019Article
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- Circular and Leaderless Bacteriocins: Biosynthesis, Mode of Action, Applications, and Prospects.Frontiers in microbiology · 2018Review
- Structural features of many circular and leaderless bacteriocins are similar to those in saposins and saposin-like peptides.MedChemComm · 2017Review
- The Leaderless Bacteriocin Enterocin K1 Is Highly Potent againstFrontiers in microbiology · 2017Article
- LsbB Bacteriocin Interacts with the Third Transmembrane Domain of the YvjB Receptor.Applied and environmental microbiology · 2016Article
- Novel Group of Leaderless Multipeptide Bacteriocins from Gram-Positive Bacteria.Applied and environmental microbiology · 2016Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
LsbB is a class II leaderless lactococcal bacteriocin of 30 amino acids. In the present work, the structure and function relationship of LsbB was assessed. Structure determination by NMR spectroscopy showed that LsbB has an N-terminal α-helix, whereas the C-terminal of the molecule remains unstructured. To define the receptor binding domain of LsbB, a competition assay was performed in which a systematic collection of truncated peptides of various lengths covering different parts of LsbB was used to inhibit the antimicrobial activity of LsbB. The results indicate that the outmost eight-amino acid sequence at the C-terminal end is likely to contain the receptor binding domain because only truncated fragments from this region could antagonize the antimicrobial activity of LsbB. Furthermore, alanine substitution revealed that the tryptophan in position 25 (Trp(25)) is crucial for the blocking activity of the truncated peptides, as well as for the antimicrobial activity of the full-length bacteriocin. LsbB shares significant sequence homology with five other leaderless bacteriocins, especially at their C-terminal halves where all contain a conserved KXXXGXXPWE motif, suggesting that they might recognize the same receptor as LsbB. This notion was supported by the fact that truncated peptides with sequences derived from the C-terminal regions of two LsbB-related bacteriocins inhibited the activity of LsbB, in the same manner as found with the truncated version of LsbB. Taken together, these structure-function studies provide strong evidence that the receptor-binding parts of LsbB and sequence-related bacteriocins are located in their C-terminal halves.
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