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

Download
  1. (PDF, 3 MB)
  2. Get@NRC: Francisella tularensis IglG belongs to a novel family of PAAR-Like T6SS proteins and harbors a unique N-terminal extension required for virulence (Opens in a new window)
DOIResolve DOI: http://doi.org/10.1371/journal.ppat.1005821
AuthorSearch for: ; Search for: ; Search for: ; Search for: ; Search for: ; Search for: ; Search for: ; Search for: ; Search for: ; Search for: ; Search for: ; Search for: ; Search for: ; Search for: ; Search for:
TypeArticle
Journal titlePLoS Pathogens
ISSN1553-7366
1553-7374
Volume12
Issue9
Article numbere1005821
AbstractThe 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
PublisherPublic Library of Science
LanguageEnglish
AffiliationAutomotive and Surface Transportation; National Research Council Canada; Human Health Therapeutics
Peer reviewedYes
NPARC number23000760
Export citationExport as RIS
Report a correctionReport a correction
Record identifier246a1033-b92c-452d-a489-47f7fe1bd5f0
Record created2016-09-14
Record modified2016-09-14
Bookmark and share
  • Share this page with Facebook (Opens in a new window)
  • Share this page with Twitter (Opens in a new window)
  • Share this page with Google+ (Opens in a new window)
  • Share this page with Delicious (Opens in a new window)