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d‑Peptidase Activity in a Marine Mollusk Detoxifies a Nonribosomal Cyclic Lipopeptide: An Ecological Model to Study Antibiotic Resistance

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posted on 2021-04-29, 17:07 authored by Laurine Darcel, Louis Bornancin, Delphine Raviglione, Isabelle Bonnard, Suzanne C. Mills, Julio Sáez-Vásquez, Bernard Banaigs, Nicolas Inguimbert
In the marine environment, sessile cyanobacteria have developed chemical strategies for protection against grazers. In turn, herbivores have to circumvent these defenses and in certain cases even take advantage of them as shelter from their own predators. This is the case of Stylocheilus striatus, a sea hare that feeds on Anabaena torulosa, a cyanobacterium that produces toxic cyclic lipopeptides of the laxaphycin B family. S. striatus consumes the cyanobacterium without being affected by the toxicity of its compounds and also uses it as an invisibility cloak against predators. In this article, using different substrates analogous to laxaphycin B, we demonstrate the presence of an enzyme in the digestive gland of the mollusk that is able to biotransform laxaphycin B derivatives. The enzyme belongs to the poorly known family of d-peptidases that are suspected to be involved in antibiotic resistance.

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