{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Daher W"],"funding":["Fondation pour la Recherche Médicale (Foundation for Medical Research in France)","Agence Nationale de la Recherche (French National Research Agency)","Gouvernement du Canada | Canadian Institutes of Health Research (Instituts de Recherche en Santé du Canada)"],"pagination":["166"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11791044"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["8(1)"],"pubmed_abstract":["Type VII secretion systems participate in protein export, virulence, conjugation, and metabolic regulation. Five subtypes (ESX-1 to ESX-5) exist, each with specific roles and well-characterized secretion profiles in various mycobacterial species. Mycobacterium abscessus, encodes only ESX-3 and ESX-4. Here, single and double M. abscessus mutants lacking the main ATPases EccC3 and EccC4 were used to define ESX-3 and ESX-4 contributions to substrate secretion and virulence. Our results demonstrate that EsxG/H secretion depends entirely on ESX-3, whereas both ESX-3 and ESX-4 secrete EsxU/T. Furthermore, two newly identified PE/PPE substrates (MAB_0046/MAB_0047) require ESX-3 for secretion. Functional complementation restored secretion and revealed subpolar localization of these systems. Macrop"],"journal":["Communications biology"],"pubmed_title":["Deletion of ESX-3 and ESX-4 secretion systems in Mycobacterium abscessus results in highly impaired pathogenicity."],"pmcid":["PMC11791044"],"funding_grant_id":["19-CE15-0012-01; SUNLIVE","Antimicrobial Resistance 202309ARB","Equipe FRM EQU202103012588"],"pubmed_authors":["Parmar S","Le Moigne V","Tocheva EI","Tasrini Y","Sexton DL","Herrmann JL","Daher W","Berdal V","Aguilera-Correa JJ","Kremer L"],"additional_accession":[]},"is_claimable":false,"name":"Deletion of ESX-3 and ESX-4 secretion systems in Mycobacterium abscessus results in highly impaired pathogenicity.","description":"Type VII secretion systems participate in protein export, virulence, conjugation, and metabolic regulation. Five subtypes (ESX-1 to ESX-5) exist, each with specific roles and well-characterized secretion profiles in various mycobacterial species. Mycobacterium abscessus, encodes only ESX-3 and ESX-4. Here, single and double M. abscessus mutants lacking the main ATPases EccC3 and EccC4 were used to define ESX-3 and ESX-4 contributions to substrate secretion and virulence. Our results demonstrate that EsxG/H secretion depends entirely on ESX-3, whereas both ESX-3 and ESX-4 secrete EsxU/T. Furthermore, two newly identified PE/PPE substrates (MAB_0046/MAB_0047) require ESX-3 for secretion. Functional complementation restored secretion and revealed subpolar localization of these systems. Macrop","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Feb","modification":"2026-05-29T16:51:41.505Z","creation":"2025-04-04T00:51:48.131Z"},"accession":"S-EPMC11791044","cross_references":{"pubmed":["39900631"],"doi":["10.1038/s42003-025-07572-4"]}}