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Alterins Produced by Oyster-Associated Pseudoalteromonas Are Antibacterial Cyclolipopeptides with LPS-Binding Activity

Laboratoire de Biotechnologie et Chimie Marine, EA3884, Université de Bretagne Occidentale, Université Bretagne Sud, 29334 Quimper, France
Institut des Sciences Chimiques de Rennes-CNRS-UMR 6226, Université Rennes, 35043 Rennes, France
IRCM, Institut de Recherche en Cancérologie de Montpellier, INSERM U1194, Université de Montpellier, Institut régional du Cancer de Montpellier, 34298 Montpellier, France
MARBEC Université de Montpellier, CNRS, IRD, Place Eugène Bataillon CC 093, Place Eugène Bataillon, CEDEX 5, 34095 Montpellier, France
Interactions Hôtes-Pathogènes-Environnements, Université de Montpellier, CNRS, Ifremer, Université Perpignan Via Domitia, 34095 Montpellier, France
Author to whom correspondence should be addressed.
Present address: Univ Caen Normandie—Unité de Recherche Risques Microbiens EA 4655, 14032 Caen, France.
Present address: IRMB, CARTIGEN, CHU de Montpellier, 34090 Montpellier, France.
Mar. Drugs 2020, 18(12), 630;
Received: 17 November 2020 / Revised: 3 December 2020 / Accepted: 7 December 2020 / Published: 10 December 2020
(This article belongs to the Special Issue Marine Antibiotics 2020)
Discovery after discovery, host-associated microbiota reveal a growing list of positive effects on host homeostasis by contributing to host nutrition, improving hosts’ immune systems and protecting hosts against pathogens. In that context, a collection of oyster associated bacteria producing antibacterial compounds have been established to evaluate their role in non-host-derived immunity. Here, we described alterins; potent anti-Gram negative compounds produced by Pseudoalteromonas hCg-6 and hCg-42 isolated from different healthy oyster hemolymph. The strains hCg-6 and hCg-42 produce a set of at least seven antibacterial compounds, ranging from 926 to 982 Da structurally characterized as cyclolipopeptides (CLPs). Alterins share the same cationic heptapeptidic cycle connected via an amido bond to different hydrophobic hydrocarbon tails. Their MICs disclosed a potent antibacterial activity directed against Gram-negative bacteria including oyster and human pathogens that may confer a beneficial defense mechanism to the host but also represents an untapped source of new antibiotics. The alterins’ mechanisms of action have been deciphered: after binding to lipopolysaccharides (LPS), alterins provoke a membrane depolarization and permeabilization leading to bacterial lysis. As hCg-6 and hCg-42 produced a set of natural derivatives, the structure/activity relationship linked to the carbon tail is clarified. We showed that the hydrocarbon tail determines the LPS-binding properties of alterins and consequently their antibacterial activities. Its length and saturation seem to play a major role in this interaction. View Full-Text
Keywords: Pseudoalteromonas; cyclolipopeptides; alterin; antibiotic Pseudoalteromonas; cyclolipopeptides; alterin; antibiotic
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MDPI and ACS Style

Desriac, F.; El Harras, A.; Simon, M.; Bondon, A.; Brillet, B.; Le Chevalier, P.; Pugnière, M.; Got, P.; Destoumieux-Garzón, D.; Fleury, Y. Alterins Produced by Oyster-Associated Pseudoalteromonas Are Antibacterial Cyclolipopeptides with LPS-Binding Activity. Mar. Drugs 2020, 18, 630.

AMA Style

Desriac F, El Harras A, Simon M, Bondon A, Brillet B, Le Chevalier P, Pugnière M, Got P, Destoumieux-Garzón D, Fleury Y. Alterins Produced by Oyster-Associated Pseudoalteromonas Are Antibacterial Cyclolipopeptides with LPS-Binding Activity. Marine Drugs. 2020; 18(12):630.

Chicago/Turabian Style

Desriac, Florie, Abderrafek El Harras, Matthieu Simon, Arnaud Bondon, Benjamin Brillet, Patrick Le Chevalier, Martine Pugnière, Patrice Got, Delphine Destoumieux-Garzón, and Yannick Fleury. 2020. "Alterins Produced by Oyster-Associated Pseudoalteromonas Are Antibacterial Cyclolipopeptides with LPS-Binding Activity" Marine Drugs 18, no. 12: 630.

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