ArticleProtein science : a publication of the Protein Society2016
Spa47 is an oligomerization-activated type three secretion system (T3SS) ATPase from Shigella flexneri.
Article in Protein science : a publication of the Protein Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
19 citing papers in PubMed, 23 citations in OpenAlex.
- Structural and Biophysical Characterization of the Yersinia Type Three Secretion System ATPase YscN.Proteins · 2026Article
- Protocol for performing and optimizing differential scanning fluorimetry experiments.STAR protocols · 2023Article
- Differential regulation ofFrontiers in cellular and infection microbiology · 2023Article
- Assembly and architecture of the type III secretion sorting platform.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Phosphomimetic Tyrosine Mutations in Spa47 Inhibit Type Three Secretion ATPase Activity andPathogens (Basel, Switzerland) · 2022Article
- Delineating specific regions of N- terminal domain of T3SS ATPase YsaN ofFrontiers in molecular biosciences · 2022Article
- Article
- TheMicroorganisms · 2021Review
- Article
- Novel Noncompetitive Type Three Secretion System ATPase Inhibitors Shut DownBiochemistry · 2020Article
- Dominant negative effects by inactive Spa47 mutants inhibit T3SS function and Shigella virulence.PloS one · 2020Article
- Interfacial amino acids support Spa47 oligomerization and shigella type three secretion system activation.Proteins · 2019Article
- Structural analysis of ligand-bound states of the Salmonella type III secretion system ATPase InvC.Protein science : a publication of the Protein Society · 2019Article
- Cryo-EM structure of the homohexameric T3SS ATPase-central stalk complex reveals rotary ATPase-like asymmetry.Nature communications · 2019Article
- Shutting Down Shigella Secretion: Characterizing Small Molecule Type Three Secretion System ATPase Inhibitors.Biochemistry · 2018Article
- Kinetic Characterization of theBio-protocol · 2018Article
- MxiN Differentially Regulates Monomeric and Oligomeric Species of the Shigella Type Three Secretion System ATPase Spa47.Biochemistry · 2018Article
- Structural Insight Into Conformational Changes Induced by ATP Binding in a Type III Secretion-Associated ATPase FromFrontiers in microbiology · 2018Article
- Structural and Biochemical Characterization of Spa47 Provides Mechanistic Insight into Type III Secretion System ATPase Activation and Shigella Virulence Regulation.The Journal of biological chemistry · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Gram-negative pathogens often use conserved type three secretion systems (T3SS) for virulence. The Shigella type three secretion apparatus (T3SA) penetrates the host cell membrane and provides a unidirectional conduit for injection of effectors into host cells. The protein Spa47 localizes to the base of the apparatus and is speculated to be an ATPase that provides the energy for T3SA formation and secretion. Here, we developed an expression and purification protocol, producing active Spa47 and providing the first direct evidence that Spa47 is a bona fide ATPase. Additionally, size exclusion chromatography and analytical ultracentrifugation identified multiple oligomeric species of Spa47 with the largest greater than 8 fold more active for ATP hydrolysis than the monomer. An ATPase inactive Spa47 point mutant was then engineered by targeting a conserved Lysine within the predicted Walker A motif of Spa47. Interestingly, the mutant maintained a similar oligomerization pattern as active Spa47, but was unable to restore invasion phenotype when used to complement a spa47 null S. flexneri strain. Together, these results identify Spa47 as a Shigella T3SS ATPase and suggest that its activity is linked to oligomerization, perhaps as a regulatory mechanism as seen in some related pathogens. Additionally, Spa47 catalyzed ATP hydrolysis appears to be essential for host cell invasion, providing a strong platform for additional studies dissecting its role in virulence and providing an attractive target for anti-infective agents.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.