ArticlePLoS pathogens2016
Francisella tularensis IglG Belongs to a Novel Family of PAAR-Like T6SS Proteins and Harbors a Unique N-terminal Extension Required for Virulence.
Article in PLoS pathogens, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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37 citing papers in PubMed, 45 citations in OpenAlex.
- Structure and potential role of T6SS effector PdpC in Francisella tularensis intracellular lifestyle.Communications biology · 2026Article
- An ubiquitous antibacterial toxin from human gut bacteria engenders neonatal colonization advantage.Nature communications · 2026Article
- Atomic Structure and Phospholipid Binding Properties of thebioRxiv : the preprint server for biology · 2025Article
- Identification of theFrontiers in cellular and infection microbiology · 2025Article
- Proteogenomic annotation of T6SS components identified inFrontiers in microbiology · 2025Article
- A type VI secretion system effector TseG of Pantoea ananatis is involved in virulence and antibacterial activity.Molecular plant pathology · 2024Article
- Breaking the cellular defense: the role of autophagy evasion inFrontiers in cellular and infection microbiology · 2024Article
- Pathogenicity and virulence ofVirulence · 2023Review
- Killing in the name of: T6SS structure and effector diversity.Microbiology (Reading, England) · 2023Review
- Recruitment of heterologous substrates by bacterial secretion systems for transkingdom translocation.Frontiers in cellular and infection microbiology · 2023Review
- Pathogenicity and virulence ofVirulence · 2022Review
- Atomic Structure of IglD Demonstrates Its Role as a Component of the Baseplate Complex of themBio · 2022Article
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- Amoebae can promote the survival ofEmerging microbes & infections · 2021Article
- An AraC/XylS Family Transcriptional Regulator Modulates the Oxidative Stress Response of Francisella tularensis.Journal of bacteriology · 2021Article
- The Breadth and Molecular Basis of Hcp-Driven Type VI Secretion System Effector Delivery.mBio · 2021Article
- Bioinformatic Analysis of theFrontiers in microbiology · 2021Article
- OpiA, a Type Six Secretion System Substrate, Localizes to the Cell Pole and Plays a Role in Bacterial Growth and Viability inJournal of bacteriology · 2020Article
- Article
- Atomic Structure of the Francisella T6SS Central Spike Reveals a Unique α-Helical Lid and a Putative Cargo.Structure (London, England : 1993) · 2019Article
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15 authors at 8 institutions in 3 countries.
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No grant is acknowledged in the PubMed record.
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.
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