ArticlePloS one2013
Structure-Function Analysis of DipA, a Francisella tularensis Virulence Factor Required for Intracellular Replication.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 23 citations in OpenAlex.
- Diversity and structural-functional insights of alpha-solenoid proteins.Protein science : a publication of the Protein Society · 2024Review
- Structural and biophysical properties of FopA, a major outer membrane protein of Francisella tularensis.PloS one · 2022Article
- Role ofAntibiotics (Basel, Switzerland) · 2021Article
- APathogens (Basel, Switzerland) · 2020Article
- Isolation ofFrontiers in cellular and infection microbiology · 2017Article
- The Multiple Localized Glyceraldehyde-3-Phosphate Dehydrogenase Contributes to the Attenuation of theFrontiers in cellular and infection microbiology · 2017Article
- The orange spotted cockroach (Proceedings of the West Virginia Academy of Science · 2017Article
- Identification and Characterization of msf, a Novel Virulence Factor in Haemophilus influenzae.PloS one · 2016Article
- Francisella tularensis type B ΔdsbA mutant protects against type A strain and induces strong inflammatory cytokine and Th1-like antibody response in vivo.Pathogens and disease · 2015Article
- Identifying Francisella tularensis genes required for growth in host cells.Infection and immunity · 2015Article
- From the Outside-In: The Francisella tularensis Envelope and Virulence.Frontiers in cellular and infection microbiology · 2015Review
- Characterization of tetratricopeptide repeat-like proteins in Francisella tularensis and identification of a novel locus required for virulence.Infection and immunity · 2014Article
- Identification of disulfide bond isomerase substrates reveals bacterial virulence factors.Molecular microbiology · 2014Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Francisella tularensis is a highly infectious bacterium whose virulence relies on its ability to rapidly reach the macrophage cytosol and extensively replicate in this compartment. We previously identified a novel Francisella virulence factor, DipA (FTT0369c), which is required for intramacrophage proliferation and survival, and virulence in mice. DipA is a 353 amino acid protein with a Sec-dependent signal peptide, four Sel1-like repeats (SLR), and a C-terminal coiled-coil (CC) domain. Here, we determined through biochemical and localization studies that DipA is a membrane-associated protein exposed on the surface of the prototypical F. tularensis subsp. tularensis strain SchuS4 during macrophage infection. Deletion and substitution mutagenesis showed that the CC domain, but not the SLR motifs, of DipA is required for surface exposure on SchuS4. Complementation of the dipA mutant with either DipA CC or SLR domain mutants did not restore intracellular growth of Francisella, indicating that proper localization and the SLR domains are required for DipA function. Co-immunoprecipitation studies revealed interactions with the Francisella outer membrane protein FopA, suggesting that DipA is part of a membrane-associated complex. Altogether, our findings indicate that DipA is positioned at the host-pathogen interface to influence the intracellular fate of this pathogen.
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