Siderophore Peptide, a New Type of Post-translationally Modified Antibacterial Peptide with Potent Activity

Thomas, Xavier; Destoumieux-Garzón, Delphine; Péduzzi, J.; Afonso, Carlos; Blond, Alain; Birlirakis, Nicolas; Goulard, Christophe; Dubost, Lionel; Thaï, Robert; Tabet, Jean‐Claude; Rebuffat, Sylvie

doi:10.1074/jbc.m400228200

Cited by 141 publications

(195 citation statements)

References 44 publications

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“…Bioassays were performed with the bacterial strains described previously [21,22], as well as with S. enterica Paratyphi SL369 [23], S. enterica Typhimurium LT2 [23], P. agglomerans K4 [24] (generously provided by Professor Volkmar Braun, University of Tübingen, Germany) and Pseudomonas aeruginosa A.T.C.C. 27853 (a gift from Professor Alain Reynaud, Hospital of Nantes, France).…”

Section: Micro-organismsmentioning

confidence: 99%

The iron–siderophore transporter FhuA is the receptor for the antimicrobial peptide microcin J25: role of the microcin Val11–Pro16 β-hairpin region in the recognition mechanism

Destoumieux-Garzón

Duquesne

Péduzzi

et al. 2005

Biochemical Journal

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122

109

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The role of the outer-membrane iron transporter FhuA as a potential receptor for the antimicrobial peptide MccJ25 (microcin J25) was studied through a series of in vivo and in vitro experiments. The requirement for both FhuA and the inner-membrane TonB-ExbB-ExbD complex was demonstrated by antibacterial assays using complementation of an fhuA − strain and by using isogenic strains mutated in genes encoding the protein complex respectively.

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Section: Micro-organismsmentioning

confidence: 99%

The iron–siderophore transporter FhuA is the receptor for the antimicrobial peptide microcin J25: role of the microcin Val11–Pro16 β-hairpin region in the recognition mechanism

Destoumieux-Garzón

Duquesne

Péduzzi

et al. 2005

Biochemical Journal

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122

109

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“…For matrix-assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF MS) determinations and immunoblotting, MccE492 was extracted from 500 ml of the supernatant from cultures of E. coli VCS257(DE3) carrying the corresponding plasmid using a procedure similar to that described previously (5). The cells were diluted 10,000 to 100,000 and grown at 37°C in M9 minimal medium supplemented with citrate and glucose (26) with 220 rpm shaking for 20 h, and the supernatant was collected by centrifugation at 17,000 ϫ g for 30 min.…”

Section: Methodsmentioning

confidence: 99%

“…Glycosylation of enterochelin [the cyclic trimer of N- (2,3-dihydroxybenzoyl)-L-serine (DHBS)] and its derivatives give rise to molecules collectively known as salmochelinlike molecules (6,7). Thus, MccE492 can be modified with a linear trimer of DHBS linked to the serine-84 carboxylate through a ␤-D-glucose moiety (8,718 Da) and also with derivatives involving a DHBS dimer (8,495 Da) and monomer (8,272 Da) (5). MccE492 modified with the diglycosylated DHBS trimer is also found (8,880 Da).…”

mentioning

confidence: 99%

“…The group of genes necessary for the production of active MccE492 has been cloned and expressed in Escherichia coli (3,4). This bacteriocin is found in two forms, unmodified (7,887 Da) and posttranslationally modified by the covalent linkage of salmochelin-like molecules of different molecular masses (5). Glycosylation of enterochelin [the cyclic trimer of N- (2,3-dihydroxybenzoyl)-L-serine (DHBS)] and its derivatives give rise to molecules collectively known as salmochelinlike molecules (6,7).…”

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confidence: 99%

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Microcin E492 Amyloid Formation Is Retarded by Posttranslational Modification

Marcoleta

Marín

Mercado

et al. 2013

Journal of Bacteriology

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b Microcin E492, a channel-forming bacteriocin with the ability to form amyloid fibers, is exported as a mixture of two forms: unmodified (inactive) and posttranslationally modified at the C terminus with a salmochelin-like molecule, which is an essential modification for conferring antibacterial activity. During the stationary phase, the unmodified form accumulates because expression of the maturation genes mceIJ is turned off, and microcin E492 is rapidly inactivated. The aim of this work was to demonstrate that the increase in the proportion of unmodified microcin E492 augments the ability of this bacteriocin to form amyloid fibers, which in turn decreases antibacterial activity. To this end, strains with altered proportions of the two forms were constructed. The increase in the expression of the maturation genes augmented the antibacterial activity during all growth phases and delayed the loss of activity in the stationary phase, while the ability to form amyloid fibers was markedly reduced. Conversely, a higher expression of microcin E492 protein produced concomitant decreases in the levels of the modified form and in antibacterial activity and a substantial increase in the ability to form amyloid fibers. The same morphology for these fibers, including those formed by only the unmodified version, was observed. Moreover, seeds formed using exclusively the nonmodified form were remarkably more efficient in amyloid formation with a shorter lag phase, indicating that the nucleation process is probably improved. Unmodified microcin E492 incorporation into amyloid fibers was kinetically more efficient than the modified form, probably due to the existence of a conformation that favors this process.

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“…Microbial siderophore transport mechanisms are also targets of a new class of antibiotics, termed siderophore-peptides, which tether anti-microbial peptides of the microcin class to the enterobactin family of siderophores (Thomas et al, 2004). This Trojan horse strategy allows bacteria to eliminate competitors that use any of several different transporters for enterobactin-like siderophores.…”

Section: Introductionmentioning

confidence: 99%

Iron metabolism at the host pathogen interface: Lipocalin 2 and the pathogen-associated iroA gene cluster

Smith

2007

The International Journal of Biochemistry & Cell Biology

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The host innate immune defense protein lipocalin 2 binds bacterial enterobactin siderophores to limit bacterial iron acquisition. To counteract this host defense mechanism bacteria have acquired the iroA gene cluster, which encodes enzymatic machinery and transporters that revitalize enterobactin in the form of salmochelin. The iroB enzyme introduces glucosyl residues at the C5 site on 2,3-dihydroxybenzoylserine moieties of enterobactin and thereby prevents lipocalin 2 binding. Additional strategies to evade lipocalin 2 have evolved in other bacteria, such as Mycobacteria tuberculosis and Bacillus anthracis. Targeting these specialized bacterial evasion strategy may provide a mechanism to reinvigorate lipocalin 2 in defense against specific pathogens.

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Siderophore Peptide, a New Type of Post-translationally Modified Antibacterial Peptide with Potent Activity

Cited by 141 publications

References 44 publications

The iron–siderophore transporter FhuA is the receptor for the antimicrobial peptide microcin J25: role of the microcin Val11–Pro16 β-hairpin region in the recognition mechanism

The iron–siderophore transporter FhuA is the receptor for the antimicrobial peptide microcin J25: role of the microcin Val11–Pro16 β-hairpin region in the recognition mechanism

Microcin E492 Amyloid Formation Is Retarded by Posttranslational Modification

Iron metabolism at the host pathogen interface: Lipocalin 2 and the pathogen-associated iroA gene cluster

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