ArticleMicrobial biotechnology2018
Exploring bioactive peptides from bacterial secretomes using PepSAVI-MS: identification and characterization of Bac-21 from Enterococcus faecalis pPD1.
Article in Microbial biotechnology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Secretome analysis of an environmental isolate Enterobacter sp. S-33 identifies proteins related to pathogenicity.Archives of microbiology · 2022Article
- Creating optimized peptide libraries for AMP discovery via PepSAVI-MS.Methods in enzymology · 2022Article
- Implementation of Microfluidics for Antimicrobial Susceptibility Assays: Issues and Optimization Requirements.Frontiers in cellular and infection microbiology · 2020Article
- PepSAVI-MS Reveals a Proline-rich Antimicrobial Peptide inJournal of natural products · 2019Article
- Exploring bioactive peptides from bacterial secretomes using PepSAVI-MS: identification and characterization of Bac-21 from Enterococcus faecalis pPD1.Microbial biotechnology · 2018Article
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Authors and funding
9 authors.
Funding
Abstract
As current methods for antibiotic drug discovery are being outpaced by the rise of antimicrobial resistance, new methods and innovative technologies are necessary to replenish our dwindling arsenal of antimicrobial agents. To this end, we developed the PepSAVI-MS pipeline to expedite the search for natural product bioactive peptides. Herein we demonstrate expansion of PepSAVI-MS for the discovery of bacterial-sourced bioactive peptides through identification of the bacteriocin Bac-21 from Enterococcus faecalis pPD1. Minor pipeline modifications including implementation of bacteria-infused agar diffusion assays and optional digestion of peptide libraries highlight the versatility and wide adaptability of the PepSAVI-MS pipeline. Additionally, we have experimentally validated the primary protein sequence of the active, mature Bac-21 peptide for the first time and have confirmed its identity with respect to primary sequence and post-translational processing. Successful application of PepSAVI-MS to bacterial secretomes as demonstrated herein establishes proof-of-principle for use in novel microbial bioactive peptide discovery.
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