Cited by 128Antimicrobial Peptides and ActivitiesMicrobial Natural Products and BiosynthesisBacterial Genetics and Biotechnology

Isolation and Characterization of Two Members of the Siderophore-Microcin Family, Microcins M and H47

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Vassiliadis, Gaëlle, Destoumieux-Garzón, Delphine, Lombard, Carine, Rebuffat, Sylvie, Peduzzi, Jean·2010·Antimicrobial Agents and Chemotherapy

Abstract

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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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)
Venue
Antimicrobial Agents and Chemotherapy
Published
2010-01
Volume
54
Issue
1
Pages
288-297
ISSN
  • 0066-4804 (ISSN-L)
  • 1098-6596
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
Locations
  • Antimicrobial Agents and Chemotherapy (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
  • Health Sciences › Medicine › Pharmacology › 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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