ORCID

https://orcid.org/0000-0001-8215-1387

Document Type

Review

Creative Commons License

Creative Commons Attribution 4.0 International License
This work is licensed under a Creative Commons Attribution 4.0 International License.

Disciplines

Biology | Life Sciences

Publication Details

Scientific Reports

© 2020 Authors

Abstract

Nisin P is a natural nisin variant, the genetic determinants for which were previously identifed in the genomes of two Streptococcus species, albeit with no confrmed evidence of production. Here we describe Streptococcus agalactiae DPC7040, a human faecal isolate, which exhibits antimicrobial activity against a panel of gut and food isolates by virtue of producing nisin P. Nisin P was purifed, and its predicted structure was confrmed by nanoLC-MS/MS, with both the fully modifed peptide and a variant without rings B and E being identifed. Additionally, we compared its spectrum of inhibition and minimum inhibitory concentration (MIC) with that of nisin A and its antimicrobial efect in a faecal fermentation in comparison with nisin A and H. We found that its antimicrobial activity was less potent than nisin A and H, and we propose a link between this reduced activity and the peptide structure.

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