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Publication Abstract from PubMed

Multidrug-resistant bacteria pose serious problems in hospital-acquired infections (HAIs). Most antibiotic resistance genes are acquired via conjugative gene transfer, mediated by type 4 secretion systems (T4SS). Although most multidrug-resistant bacteria responsible for HAIs are of Gram-positive origin, with enterococci being major contributors, mostly Gram-negative T4SSs have been characterized. Here, we describe the structure and organization of PrgL, a core protein of the T4SS channel, encoded by the pCF10 plasmid from Enterococcus faecalis. The structure of PrgL displays similarity to VirB8 proteins of Gram-negative T4SSs. In vitro experiments show that the soluble domain alone is enough to drive both dimerization and dodecamerization, with a dimerization interface that differs from all other known VirB8-like proteins. In vivo experiments verify the importance of PrgL dimerization. Our findings provide insight into the molecular building blocks of Gram-positive T4SS, highlighting similarities but also unique features in PrgL compared to other VirB8-like proteins.

Structure of the enterococcal T4SS protein PrgL reveals unique dimerization interface in the VirB8 protein family.,Jager F, Lamy A, Sun WS, Guerini N, Berntsson RP Structure. 2022 Apr 6. pii: S0969-2126(22)00094-6. doi:, 10.1016/j.str.2022.03.013. PMID:35429437^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.