ArticleProtein science : a publication of the Protein Society2007
Conformational stability and differential structural analysis of LcrV, PcrV, BipD, and SipD from type III secretion systems.
Article in Protein science : a publication of the Protein Society, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Antigen-specific IgA B memory cell responses to Shigella antigens elicited in volunteers immunized with live attenuated Shigella flexneri 2a oral vaccine candidates.Clinical immunology (Orlando, Fla.) · 2011Trial
- Determination of Conformational and Functional Stability of Potential Plague Vaccine Candidate in Formulation.Vaccines · 2022Article
- Development of a Broadly Protective, Self-Adjuvanting Subunit Vaccine to Prevent Infections byFrontiers in immunology · 2020Article
- The cytoplasmic portion of the T3SS inner membrane ring components sort into distinct families based on biophysical properties.Biochimica et biophysica acta. Proteins and proteomics · 2019Article
- Single-domain antibodies pinpoint potential targets withinThe Journal of biological chemistry · 2017Article
- Type III Secretion in the Melioidosis PathogenFrontiers in cellular and infection microbiology · 2017Review
- Macrophage Apoptosis Triggered by IpaD from Shigella flexneri.Infection and immunity · 2016Article
- Key steps in type III secretion system (T3SS) towards translocon assembly with potential sensor at plant plasma membrane.Molecular plant pathology · 2015Review
- Biophysical characterization of the type III secretion tip proteins and the tip proteins attached to bacterium-like particles.Journal of pharmaceutical sciences · 2015Article
- B lymphocytes undergo TLR2-dependent apoptosis upon Shigella infection.The Journal of experimental medicine · 2014Article
- PcrG protects the two long helical oligomerization domains of PcrV, by an interaction mediated by the intramolecular coiled-coil region of PcrG.BMC structural biology · 2014Article
- Chlamydia pneumoniae CopD translocator protein plays a critical role in type III secretion (T3S) and infection.PloS one · 2014Article
- N-terminus of IpaB provides a potential anchor to the Shigella type III secretion system tip complex protein IpaD.Biochemistry · 2013Article
- The structures of coiled-coil domains from type III secretion system translocators reveal homology to pore-forming toxins.Journal of molecular biology · 2012Article
- Identification of the bile salt binding site on IpaD from Shigella flexneri and the influence of ligand binding on IpaD structure.Proteins · 2012Article
- Crystal structure of PrgI-SipD: insight into a secretion competent state of the type three secretion system needle tip and its interaction with host ligands.PLoS pathogens · 2011Article
- The Burkholderia pseudomallei type III secretion system and BopA are required for evasion of LC3-associated phagocytosis.PloS one · 2011Article
- Near-atomic resolution analysis of BipD, a component of the type III secretion system of Burkholderia pseudomallei.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010Article
- Biophysical characterization of Chlamydia trachomatis CT584 supports its potential role as a type III secretion needle tip protein.Biochemistry · 2009Article
- Structural dissection of the extracellular moieties of the type III secretion apparatus.Molecular bioSystems · 2008Review
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Abstract
Diverse Gram-negative bacteria use type III secretion systems (T3SS) to translocate effector proteins into the cytoplasm of eukaryotic cells. The type III secretion apparatus (T3SA) consists of a basal body spanning both bacterial membranes and an external needle. A sensor protein lies at the needle tip to detect environmental signals that trigger type III secretion. The Shigella flexneri T3SA needle tip protein, invasion plasmid antigen D (IpaD), possesses two independently folding domains in vitro. In this study, the solution behavior and thermal unfolding properties of IpaD's functional homologs SipD (Salmonella spp.), BipD (Burkholderia pseudomallei), LcrV (Yersinia spp.), and PcrV (Pseudomonas aeruginosa) were examined to identify common features within this protein family. CD and FTIR data indicate that all members within this group are alpha-helical with properties consistent with an intramolecular coiled-coil. SipD showed the most complex unfolding profile consisting of two thermal transitions, suggesting the presence of two independently folding domains. No evidence of multiple folding domains was seen, however, for BipD, LcrV, or PcrV. Thermal studies, including DSC, revealed significant destabilization of LcrV, PcrV, and BipD after N-terminal deletions. This contrasted with SipD and IpaD, which behaved like two-domain proteins. The results suggest that needle tip proteins share significant core structural similarity and thermal stability that may be the basis for their common function. Moreover, IpaD and SipD possess properties that distinguish them from the other tip proteins.
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