A glycosylated lipooctapeptide promotes uptake and growth of Mycobacterium abscessus in the host

Louis David Leclercq, Vincent Moigne, Wassim Daher, Mélanie Cortes, Bertus Viljoen, Yara Tasrini, Xavier Trivelli, Hélène Lavanant, Isabelle Schmitz-Afonso, Nicolas Durand, Franck Biet, Yann Guérardel (), Laurent Kremer () and Jean-Louis Herrmann ()
Additional contact information
Louis David Leclercq: UMR 8576—UGSF—Unité de Glycobiologie Structurale et Fonctionnelle
Vincent Moigne: Université Paris-Saclay, UVSQ, Inserm, Infection et inflammation
Wassim Daher: Université de Montpellier
Mélanie Cortes: Université Paris-Saclay, UVSQ, Inserm, Infection et inflammation
Bertus Viljoen: Université de Montpellier
Yara Tasrini: Université de Montpellier
Xavier Trivelli: Université d’Artois, FR 2638—IMEC—Institut Michel-Eugène Chevreul
Hélène Lavanant: Normandie Univ, Univ Rouen Normandie, CNRS, CARMeN UMR 6064 (ex-COBRA-LCMT)
Isabelle Schmitz-Afonso: Normandie Univ, Univ Rouen Normandie, CNRS, CARMeN UMR 6064 (ex-COBRA-LCMT)
Nicolas Durand: Université Paris-Saclay, UVSQ, Inserm, Infection et inflammation
Franck Biet: Université de Tours
Yann Guérardel: UMR 8576—UGSF—Unité de Glycobiologie Structurale et Fonctionnelle
Laurent Kremer: Université de Montpellier
Jean-Louis Herrmann: Université Paris-Saclay, UVSQ, Inserm, Infection et inflammation

Nature Communications, 2025, vol. 16, issue 1, 1-16

Abstract: Abstract Pathogenic mycobacteria produce a wide array of lipids which participate in host cell interactions and virulence. While some of these are conserved across all mycobacteria, others, like glycopeptidolipids (GPL), are restricted to a few species. Mycobacterium abscessus, an emerging rapid-growing pathogen, transitions from a smooth to a virulent rough variant upon the loss of surface GPL. Here, we discovered that M. abscessus and phylogenetically-close species harbor a second GPL-related locus, comprising two adjacent non-ribosomal peptide synthetase genes, MAB_4690c and MAB_4691c. A MAB_4690c deletion mutant (ΔMAB_4690c) failed to produce a yet undescribed lipid, designated GL8P for glycosylated lipooctapeptide, sharing an acylated octapeptide core adorned by mono or di-O-rhamnosyl substituents. ΔMAB_4690c exhibited impaired uptake and survival in THP-1 cells and was attenuated in mice. Importantly, GL8P elicited a strong humoral response in patients infected with M. abscessus. These results highlight the role of GL8P in the pathophysiology of infection by rough M. abscessus and suggest its potential as a selective marker for M. abscessus infections.

Date: 2025
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DOI: 10.1038/s41467-025-58455-5

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