ArticleBiochemistry2012
Binding affects the tertiary and quaternary structures of the Shigella translocator protein IpaB and its chaperone IpgC.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Class II chaperones: indispensable components of the Gram-negative bacterial T3SS as guardians of translocators.Archives of microbiology · 2026Review
- Development of a NovelVaccines · 2026Article
- Crystallographic Fragment Screening on theACS omega · 2023Article
- Exploring the "N-Terminal Anchor" Binding Interface of the T3SS Chaperone-Translocator Complexes fromBiochemistry · 2023Article
- Phosphomimetic Tyrosine Mutations in Spa47 Inhibit Type Three Secretion ATPase Activity andPathogens (Basel, Switzerland) · 2022Article
- HSV-1 ICP22 Is a Selective Viral Repressor of Cellular RNA Polymerase II-Mediated Transcription Elongation.Vaccines · 2021Article
- TheMicroorganisms · 2021Review
- Structural Insights ofFrontiers in cellular and infection microbiology · 2021Article
- Novel Noncompetitive Type Three Secretion System ATPase Inhibitors Shut DownBiochemistry · 2020Article
- Using disruptive insertional mutagenesis to identify the in situ structure-function landscape of the Shigella translocator protein IpaB.Protein science : a publication of the Protein Society · 2018Article
- Genetic Dissection of the Signaling Cascade that Controls Activation of the Shigella Type III Secretion System from the Needle Tip.Scientific reports · 2016Article
- Characterization of the Shigella and Salmonella Type III Secretion System Tip-Translocon Protein-Protein Interaction by Paramagnetic Relaxation Enhancement.Chembiochem : a European journal of chemical biology · 2016Article
- The Many Faces of IpaB.Frontiers in cellular and infection microbiology · 2016Review
- Chlamydia Outer Protein (Cop) B from Chlamydia pneumoniae possesses characteristic features of a type III secretion (T3S) translocator protein.BMC microbiology · 2015Article
- Article
- A gatekeeper chaperone complex directs translocator secretion during type three secretion.PLoS pathogens · 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
- Studies of the conformational stability of invasion plasmid antigen B from Shigella.Protein science : a publication of the Protein Society · 2013Article
- Oligomeric states of the Shigella translocator protein IpaB provide structural insights into formation of the type III secretion translocon.Protein science : a publication of the Protein Society · 2013Article
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8 authors.
Funding
Abstract
Shigella flexneri uses its type III secretion system (T3SS) to promote invasion of human intestinal epithelial cells as the first step in causing shigellosis, a life-threatening form of dysentery. The Shigella type III secretion apparatus (T3SA) consists of a basal body that spans the bacterial envelope and an exposed needle that injects effector proteins into target cells. The nascent Shigella T3SA needle is topped with a pentamer of the needle tip protein invasion plasmid antigen D (IpaD). Bile salts trigger recruitment of the first hydrophobic translocator protein, IpaB, to the tip complex where it senses contact with a host membrane. In the bacterial cytoplasm, IpaB exists in a complex with its chaperone IpgC. Several structures of IpgC have been determined, and we recently reported the 2.1 Å crystal structure of the N-terminal domain (IpaB(74.224)) of IpaB. Like IpgC, the IpaB N-terminal domain exists as a homodimer in solution. We now report that when the two are mixed, these homodimers dissociate and form heterodimers having a nanomolar dissociation constant. This is consistent with the equivalent complexes copurified after they had been co-expressed in Escherichia coli. Fluorescence data presented here also indicate that the N-terminal domain of IpaB possesses two regions that appear to contribute additively to chaperone binding. It is also likely that the N-terminus of IpaB adopts an alternative conformation as a result of chaperone binding. The importance of these findings within the functional context of these proteins is discussed.
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