ArticleProbiotics and antimicrobial proteins2018
Identification and Heterologous Expression of the sec-Dependent Bacteriocin Faerocin MK from Enterococcus faecium M3K31.
Article in Probiotics and antimicrobial proteins, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 10 citations in OpenAlex.
- Lactic Acid Bacteria-derived Bacteriocins: A Promising Antimicrobial Strategy against Multidrug-resistant for Neonatal Sepsis Pathogens.Probiotics and antimicrobial proteins · 2026Review
- SPI "sandwich": Combined SUMO-Peptide-Intein expression system and isolation procedure for improved stability and yield of peptides.Protein science : a publication of the Protein Society · 2022Article
- Identification and Functional Characterization of Peptides With Antimicrobial Activity From the Syphilis Spirochete,Frontiers in microbiology · 2022Article
- Overview of Global Trends in Classification, Methods of Preparation and Application of Bacteriocins.Antibiotics (Basel, Switzerland) · 2020Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Genome sequencing of Enterococcus faecium M3K31, a strain isolated from griffon vultures, previously revealed the presence of three sequences encoding for bacteriocins, namely enterocin P, enterocin HF, and a SRCAM 602-like bacteriocin. In this work, we describe the SRCAM 602-like bacteriocin that we named faerocin MK. Mature faerocin MK consists of 43 residues and contains an YGNGV-motif and two cysteine residues at positions 10 and 15, consistent with other class IIa bacteriocins. Faerocin MK and SRCAM 602 were chemically synthesized and their scope of activity was tested. Faerocin MK is active against a wide range of Gram-positive organisms while SRCAM 602 was not active against any tested organism. Although both peptides are more structured in trifluoroethanol, faerocin MK has an α-helical character nearly twice that of SRCAM 602. Nucleotide sequence analysis revealed that the faerocin MK precursor is produced with a 28-amino acid signal peptide and that an immunity gene follows the structural faerocin MK gene. Heterologous expression of the faerocin MK operon showed that faerocin MK and its immunity protein were successfully expressed in other organisms. This indicates that the bacteriocin is secreted through the sec pathway.
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