{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["299(4)"],"submitter":["Sengupta N"],"pubmed_abstract":["Mycobacterium tuberculosis (Mtb) utilizes sophisticated machinery called the type VII secretion system to translocate virulence factors across its complex lipid membrane. EspB, a ∼36 kDa secreted substrate of the ESX-1 apparatus, was shown to cause ESAT-6-independent host cell death. Despite the current wealth of high-resolution structural information of the ordered N-terminal domain, the mechanism of EspB-mediated virulence remains poorly characterized. Here, we document EspB interaction with phosphatidic acid (PA) and phosphatidylserine (PS) in the context of membranes, through a biophysical approach including transmission electron microscopy and cryo-EM. We were also able to show PA, PS-dependent conversion of monomers to oligomers at physiological pH. Our data suggest that EspB adheres"],"journal":["The Journal of biological chemistry"],"pagination":["104589"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10140165"],"repository":["biostudies-literature"],"pubmed_title":["Cryo-EM reveals the membrane-binding phenomenon of EspB, a virulence factor of the mycobacterial type VII secretion system."],"pmcid":["PMC10140165"],"pubmed_authors":["Dutta S","Sengupta N","Padmanaban S"],"additional_accession":[]},"is_claimable":false,"name":"Cryo-EM reveals the membrane-binding phenomenon of EspB, a virulence factor of the mycobacterial type VII secretion system.","description":"Mycobacterium tuberculosis (Mtb) utilizes sophisticated machinery called the type VII secretion system to translocate virulence factors across its complex lipid membrane. EspB, a ∼36 kDa secreted substrate of the ESX-1 apparatus, was shown to cause ESAT-6-independent host cell death. Despite the current wealth of high-resolution structural information of the ordered N-terminal domain, the mechanism of EspB-mediated virulence remains poorly characterized. Here, we document EspB interaction with phosphatidic acid (PA) and phosphatidylserine (PS) in the context of membranes, through a biophysical approach including transmission electron microscopy and cryo-EM. We were also able to show PA, PS-dependent conversion of monomers to oligomers at physiological pH. Our data suggest that EspB adheres","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Apr","modification":"2026-05-28T20:11:33.778Z","creation":"2025-02-19T04:45:50.181Z"},"accession":"S-EPMC10140165","cross_references":{"pubmed":["36889587"],"doi":["10.1016/j.jbc.2023.104589"]}}