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Isolation and Characterization of Two Members of the Siderophore-Microcin Family, Microcins M and H47
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In this paper we provide the first biochemical evidence of the existence of a family of structure-related antimicrobial peptides, the siderophore-microcins, in the Enterobacteriaceae family. We isolated and characterized two novel siderophore-microcins, MccM and MccH47, previously characterized through genetic studies. MccM and MccH47 were expressed from several Escherichia coli strains containing the microcin gene clusters. The spectra of their bactericidal activities were found to be restricted to some species of the Enterobacteriaceae . MccM and MccH47 were unable to inhibit the growth of strains carrying mutations in the fepA , cir , and fiu genes, which showed the requirement of the iron-catecholate receptors for their recognition. The MccM and MccH47 peptide moieties contain 77 and 60 residues, respectively, and are derived from the microcin precursors McmA and MchB, respectively. In addition, both peptides carried a C-terminal posttranslational modification containing a salmochelin-like siderophore moiety also found in MccE492 (X. Thomas et al., J. Biol. Chem., 279:28233-28242, 2004). Interestingly, when MccM was isolated from E. coli Nissle 1917, which lacks the two genes necessary for modification biosynthesis, it was devoid of posttranslational modification. Those two genes could be complemented by their homologues from the MccH47 gene cluster, thereby showing their functional interchangeability between at least two members of the siderophore-microcin family. Finally, from the sequence analysis of the MccE492 gene cluster, we hypothesized the existence of an additional member of the siderophore-microcin family. Therefore, we propose that the siderophore-microcin family contains five representatives.
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“having two plasmids (pMUT1 and pMUT2) synthetizing microcins M and H47 (active against Salmonella strains) [26, 31, 32]”
From Selection, Comparative Genomics, and Potential Probiotic Features of Escherichia coli 5C, a pks-Negative Strain Isolated from Healthy Infant Donor Feces (2026) · cites this paper as [31]
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“the strain Nissle 1917, besides the already described two microcins, known as M and H47 [31, 32], demonstrates the presence of one colicin and one bottromycin [116], both not phenotypically expressed.”
From Selection, Comparative Genomics, and Potential Probiotic Features of Escherichia coli 5C, a pks-Negative Strain Isolated from Healthy Infant Donor Feces (2026) · cites this paper as [31]
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Jones, J. A., Murphy, C. P., Sleator, R. D., & Culligan, E. P. (2024) · Microbiome Research Reports · doi:10.20517/mrr.2023.78 · Cited by 7
Bilitewski, U., Blodgett, J. A. V., Duhme‐Klair, A., Dallavalle, S., Laschat, S., Routledge, A., & Schobert, R. (2017) · Angewandte Chemie · doi:10.1002/ange.201701586 · Cited by 7
Schröder, N. C. H., Korša, A., Wami, H. T., Mantel, O., Dobrindt, U., & Kurtz, J. (2022) · Evolution Medicine and Public Health · doi:10.1093/emph/eoac001 · Cited by 6
Wyrsch, E. R., Chowdhury, P. R., Jarocki, V. M., Brandis, K., & Djordjevic, S. P. (2020) · Microbial Genomics · doi:10.1099/mgen.0.000387 · Cited by 7
Kenneally, C., Murphy, C. P., Sleator, R. D., & Culligan, E. P. (2024) · MicrobiologyOpen · doi:10.1002/mbo3.1411 · Cited by 6
Fermentative production of alternative antimicrobial peptides and enzymes
Lu, S.-Y., Skory, C. D., Enshasy, H. A. E., & Liu, S. (2021) · Biocatalysis and Agricultural Biotechnology · doi:10.1016/j.bcab.2021.102189 · Cited by 6
Mcc1229, an Stx2a-Amplifying Microcin, Is Produced In Vivo and Requires CirA for Activity
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“As regards to bacteriocin genes, the strain Nissle 1917, besides the already described two microcins, known as M and H47 [31, 32], demonstrates the presence of one colicin and one bottromycin [116], both not pheno-typically expressed.”
Jones, C. V., Jarboe, B., Majer, H. M., Ma, A. T., & Beld, J. (2021) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-021-11546-x · Cited by 5
Metadata
- Authors
- Vassiliadis, G., Destoumieux-Garzón, D., Lombard, C., Rebuffat, S., & Peduzzi, J.
- Affiliations
- Molécules de Communication et Adaptation des Micro-organismes, FRE 3206 CNRS, Muséum National d'Histoire Naturelle, CP 54, 57 rue Cuvier, Paris 75005, France
- Centre National de la Recherche Scientifique (FR)
- ORCID
- Rebuffat, Sylvie
- Venue
- Antimicrobial Agents and Chemotherapy
- Publisher
- American Society for Microbiology
- Published
- 2010-01
- Volume
- 54
- Issue
- 1
- Pages
- 288-297
- ISSN
- 0066-4804 (ISSN-L)
- 1098-6596
- PMC
- PMC2798501
- OpenAlex
- W2157624401
- Cited by
- 128
- References
- 30
- Citations by year
- 2026: 4 · 2025: 12 · 2024: 15 · 2023: 6 · 2022: 13 · 2021: 14 · 2020: 8 · 2019: 8 · 2018: 7 · 2017: 10 · 2016: 4 · 2015: 3 · 2014: 2 · 2013: 7 · 2012: 4
- FWCI
- 4.79
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Antimicrobial Agents and Chemotherapy (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
- Life Sciences › Immunology and Microbiology › Applied Microbiology and Biotechnology › Microbial Natural Products and Biosynthesis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- antimicrobial peptides, Enterobacteriaceae, Escherichia coli, FepA, CIR, post-translational modification, salmochelin, gene complementation, siderophore biosynthesis
- MeSH terms
- Amino Acid Sequence, Anti-Bacterial Agents, Bacterial Outer Membrane Proteins, Colicins, Electrophoresis, Polyacrylamide Gel, Enterobacteriaceae, Escherichia coli, Hydrolysis, Klebsiella pneumoniae, Molecular Sequence Data, Peptides, Phylogeny, Plasmids, Protein Processing, Post-Translational, Receptors, Cell Surface, Trypsin, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Antimicrobial Cationic Peptides
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