Structure of the enterococcal T4SS protein PrgL reveals unique dimerization interface in the VirB8 protein family
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 or...
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Published in | Structure (London) Vol. 30; no. 6; pp. 876 - 885.e5 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
United States
Elsevier Ltd
02.06.2022
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Subjects | |
Online Access | Get full text |
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Summary: | 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.
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•Structure of pCF10 PrgL•PrgL forms dodecamers through its soluble domain•Dimer interface is needed for in vivo function
Jäger et al. use X-ray crystallography to determine the structure of the VirB8-like protein PrgL from Enterococcus faecalis. PrgL has an unusual dimer interface that is important for both higher oligomerization and the in vivo function of the pCF10 type 4 secretion system. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0969-2126 1878-4186 1878-4186 |
DOI: | 10.1016/j.str.2022.03.013 |