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Structure of the enterococcal T4SS protein PrgL reveals unique dimerization interface in the VirB8 protein family

View ORCID ProfileFranziska Jäger, Anaïs Lamy, Nina Guerini, Wei-Sheng Sun, View ORCID ProfileRonnie P-A Berntsson
doi: https://doi.org/10.1101/2020.10.30.342212
Franziska Jäger
1Department of Medical Biochemistry and Biophysics, Umeå University, SE-90187 Umeå, Sweden
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  • ORCID record for Franziska Jäger
Anaïs Lamy
1Department of Medical Biochemistry and Biophysics, Umeå University, SE-90187 Umeå, Sweden
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Nina Guerini
1Department of Medical Biochemistry and Biophysics, Umeå University, SE-90187 Umeå, Sweden
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Wei-Sheng Sun
1Department of Medical Biochemistry and Biophysics, Umeå University, SE-90187 Umeå, Sweden
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Ronnie P-A Berntsson
1Department of Medical Biochemistry and Biophysics, Umeå University, SE-90187 Umeå, Sweden
2Wallenberg Centre for Molecular Medicine, Umeå University, Umeå, Sweden
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  • For correspondence: ronnie.berntsson@umu.se
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Abstract

Multidrug resistant bacteria are one of the most important current threats to public health and a serious problem in hospital acquired infections (HAIs). Most antibiotic resistance genes are acquired via conjugative gene transfer, in a process that is mediated by a protein machinery called the Type 4 Secretion System (T4SS). The core of the T4SS is a multiprotein complex that spans both the cell wall and cellular membrane(s), serving as a channel for macromolecular secretion. Although the majority of 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 organisation of PrgL, one of the seven membrane proteins forming the translocation channel of the T4SS encoded by the pCF10 plasmid from Enterococcus faecalis. We present the structure of the C-terminal domain of PrgL, which displays similarity to VirB8 proteins of Gram-negative secretion systems. PrgL forms dimers and higher order oligomers but does not interact strongly with the other T4SS components. In vitro experiments show that the soluble domain alone is enough to drive both dimerization and dodecamerisation, with a dimerization interface that differs from all other known VirB8-like proteins. 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.

Competing Interest Statement

The authors have declared no competing interest.

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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC-ND 4.0 International license.
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Posted October 30, 2020.
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Structure of the enterococcal T4SS protein PrgL reveals unique dimerization interface in the VirB8 protein family
Franziska Jäger, Anaïs Lamy, Nina Guerini, Wei-Sheng Sun, Ronnie P-A Berntsson
bioRxiv 2020.10.30.342212; doi: https://doi.org/10.1101/2020.10.30.342212
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Structure of the enterococcal T4SS protein PrgL reveals unique dimerization interface in the VirB8 protein family
Franziska Jäger, Anaïs Lamy, Nina Guerini, Wei-Sheng Sun, Ronnie P-A Berntsson
bioRxiv 2020.10.30.342212; doi: https://doi.org/10.1101/2020.10.30.342212

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