Francisella tularensis IglG belongs to a novel family of PAAR-Like T6SS proteins and harbors a unique N-terminal extension required for virulence

From National Research Council Canada

Download	View final version: Francisella tularensis IglG belongs to a novel family of PAAR-Like T6SS proteins and harbors a unique N-terminal extension required for virulence (PDF, 4 MB)
DOI	Resolve DOI: https://doi.org/10.1371/journal.ppat.1005821
Author	Search for: Rigard, Mélanie; Search for: Bröms, Jeanette E.; Search for: Mosnier, Amandine; Search for: Hologne, Maggy; Search for: Martin, Amandine; Search for: Lindgren, Lena; Search for: Punginelli, Claire; Search for: Lays, Claire; Search for: Walker, Olivier; Search for: Charbit, Alain; Search for: Telouk, Philippe; Search for: Conlan, Wayne¹; Search for: Terradot, Laurent; Search for: Sjöstedt, Anders; Search for: Henry, Thomas
Name affiliation	National Research Council of Canada. Human Health Therapeutics
Format	Text, Article
Journal title	PLoS Pathogens
ISSN	1553-7366 1553-7374
Volume	12
Issue	9
Article number	e1005821
Abstract	The virulence of Francisella tularensis, the etiological agent of tularemia, relies on an atypical type VI secretion system (T6SS) encoded by a genomic island termed the Francisella Pathogenicity Island (FPI). While the importance of the FPI in F. tularensis virulence is clearly established, the precise role of most of the FPI-encoded proteins remains to be deciphered. In this study, using highly virulent F. tularensis strains and the closely related species F. novicida, IglG was characterized as a protein featuring a unique α-helical N-terminal extension and a domain of unknown function (DUF4280), present in more than 250 bacterial species. Three dimensional modeling of IglG and of the DUF4280 consensus protein sequence indicates that these proteins adopt a PAAR-like fold, suggesting they could cap the T6SS in a similar way as the recently described PAAR proteins. The newly identified PAAR-like motif is characterized by four conserved cysteine residues, also present in IglG, which may bind a metal atom. We demonstrate that IglG binds metal ions and that each individual cysteine is required for T6SS-dependent secretion of IglG and of the Hcp homologue, IglC and for the F. novicida intracellular life cycle. In contrast, the Francisella-specific N-terminal α-helical extension is not required for IglG secretion, but is critical for F. novicida virulence and for the interaction of IglG with another FPI-encoded protein, IglF. Altogether, our data suggest that IglG is a PAAR-like protein acting as a bi-modal protein that may connect the tip of the Francisella T6SS with a putative T6SS effector, IglF.
Publication date	2016-09-07
Publisher	Public Library of Science
Language	English
Peer reviewed	Yes
NPARC number	23000760
Export citation	Export as RIS
Report a correction	Report a correction
Record identifier	246a1033-b92c-452d-a489-47f7fe1bd5f0
Record created	2016-09-14
Record modified	2020-06-02

Report a problem on this page

Date modified:: 2020-10-30