ArticleJournal of bacteriology2002
Shigella Spa32 is an essential secretory protein for functional type III secretion machinery and uniformity of its needle length.
Article in Journal of bacteriology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed.
- The bacterial type three secretion system induces mechanoporation of vacuolar membranes.PLoS biology · 2025Article
- TheMicroorganisms · 2021Review
- The Structure and Function of Type III Secretion Systems.Microbiology spectrum · 2016Review
- The Structure of a Type 3 Secretion System (T3SS) Ruler Protein Suggests a Molecular Mechanism for Needle Length Sensing.The Journal of biological chemistry · 2016Article
- Type Three Secretion System in Attaching and Effacing Pathogens.Frontiers in cellular and infection microbiology · 2016Review
- Article
- Bacterial iron-sulfur cluster sensors in mammalian pathogens.Metallomics : integrated biometal science · 2015Review
- Molecular ruler determines needle length for the Salmonella Spi-1 injectisome.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Genetically engineered frameshifted YopN-TyeA chimeras influence type III secretion system function in Yersinia pseudotuberculosis.PloS one · 2013Article
- Role of EscP (Orf16) in injectisome biogenesis and regulation of type III protein secretion in enteropathogenic Escherichia coli.Journal of bacteriology · 2012Article
- The non-flagellar type III secretion system evolved from the bacterial flagellum and diversified into host-cell adapted systems.PLoS genetics · 2012Article
- Needle length control and the secretion substrate specificity switch are only loosely coupled in the type III secretion apparatus of Shigella.Microbiology (Reading, England) · 2012Article
- Autoproteolysis and intramolecular dissociation of Yersinia YscU precedes secretion of its C-terminal polypeptide YscU(CC).PloS one · 2012Article
- Characterization of Salmonella type III secretion hyper-activity which results in biofilm-like cell aggregation.PloS one · 2012Article
- Structure-function analysis of the HrpB2-HrcU interaction in the Xanthomonas citri type III secretion system.PloS one · 2011Article
- A sorting platform determines the order of protein secretion in bacterial type III systems.Science (New York, N.Y.) · 2011Article
- Length control of the injectisome needle requires only one molecule of Yop secretion protein P (YscP).Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Article
- A dominant-negative needle mutant blocks type III secretion of early but not late substrates in Yersinia.Molecular microbiology · 2010Article
- Timing is everything: the regulation of type III secretion.Cellular and molecular life sciences : CMLS · 2010Review
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4 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The Shigella type III secretion machinery is responsible for delivering to host cells the set of effectors required for invasion. The type III secretion complex comprises a needle composed of MxiH and MxiI and a basal body made up of MxiD, MxiG, and MxiJ. In S. flexneri, the needle length has a narrow range, with a mean of approximately 45 nm, suggesting that it is strictly regulated. Here we show that Spa32, encoded by one of the spa genes, is an essential protein translocated via the type III secretion system and is involved in the control of needle length as well as type III secretion activity. When the spa32 gene was mutated, the type III secretion complexes possessed needles of various lengths, ranging from 40 to 1,150 nm. Upon introduction of a cloned spa32 into the spa32 mutant, the bacteria produced needles of wild-type length. The spa32 mutant overexpressing MxiH produced extremely long (>5 microm) needles. Spa32 was secreted into the medium via the type III secretion system, but secretion did not depend on activation of the system. The spa32 mutant and the mutant overexpressing MxiH did not secrete effectors such as Ipa proteins into the medium or invade HeLa cells. Upon introduction of Salmonella invJ, encoding InvJ, which has 15.4% amino acid identity with Spa32, into the spa32 mutant, the bacteria produced type III needles of wild-type length and efficiently entered HeLa cells. These findings suggest that Spa32 is an essential secreted protein for a functional type III secretion system in Shigella spp. and is involved in the control of needle length. Furthermore, its function is interchangeable with that of Salmonella InvJ.
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