Helical structure of the needle of the type III secretion system of Shigella flexneri.

Cordes, Frank; Komoriya, Kaoru; Larquet, Éric; Yang, Songfan; Blocker, Ariel; Lea, Susan M.

doi:10.1016/s0021-9258(20)83517-0

Cited by 3 publications

(2 citation statements)

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“…The helical needle is built up of more than 100 copies [74] of a small protein (PrgI/YscF/MxiH (Salmonella/Yersinia/Shigella) ,10 kDa). Native needles have a typical length varying from 30 to 70 nm and an outer diameter of about 10-13 nm [20,23,75]. Assembly of the needle filament requires first the transport to and then the polymerization of individual monomers at the distal end of the complex.…”

Section: The Extracellular Components: the Needle Filament The Tip And The Transloconmentioning

confidence: 99%

“…NMR and mutational studies showed that this turn together with the head region are involved in the MxiH interaction with the tip protein IpaD [34,82]. By positioning the crystal structure of a monomeric MxiH into a previously generated electron microscopy density map, a model was generated in which the N-terminal helix of MxiH is facing the inner channel of the filament, while the C-terminal one is suspected to be involved in its assembly [23,34].…”

Section: The Extracellular Components: the Needle Filament The Tip And The Transloconmentioning

confidence: 99%

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The blueprint of the type-3 injectisome

Kosarewicz

Königsmaier

Marlovits

2012

Phil. Trans. R. Soc. B

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Type-3 secretion systems are sophisticated syringe-like nanomachines present in many animal and plant Gram-negative pathogens. They are capable of translocating an arsenal of specific bacterial toxins (effector proteins) from the prokaryotic cytoplasm across the three biological membranes directly into the eukaryotic cytosol, some of which modulate host cell mechanisms for the benefit of the pathogen. They populate a particular biological niche, which is maintained by specific, pathogen-dependent effectors. In contrast, the needle complex, which is the central component of this specialized protein delivery machine, is structurally well-conserved. It is a large supramolecular cylindrical structure composed of multiple copies of a relatively small subset of proteins, is embedded in the bacterial membranes and protrudes from the pathogen's surface with a needle filament. A central channel traverses the entire needle complex, and serves as a hollow conduit for proteins destined to travel this secretion pathway. In the past few years, there has been a tremendous increase in an understanding on both the structural and the mechanistic level. This review will thus focus on new insights of this remarkable molecular machine.

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Section: The Extracellular Components: the Needle Filament The Tip And The Transloconmentioning

confidence: 99%

Section: The Extracellular Components: the Needle Filament The Tip And The Transloconmentioning

confidence: 99%

The blueprint of the type-3 injectisome

Kosarewicz

Königsmaier

Marlovits

2012

Phil. Trans. R. Soc. B

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Comparative transcriptomic analysis provides insights into transcription mechanisms of Vibrio parahaemolyticus T3SS during interaction with HeLa cells

Lian

Xue

et al. 2021

Braz J Microbiol

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VscF in T3SS1 Helps to Translocate VPA0226 in Vibrio parahaemolyticus

Lian

Jiao

et al. 2021

Front. Cell. Infect. Microbiol.

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In Vibrio parahaemolyticus, type III secretion system 1 (T3SS1) is a major virulence factor that delivers effectors into the host eukaryotic cytoplasm; however, studies on its infection mechanism are currently limited. To determine the function of the vscF gene, we constructed the vscF deletion mutant ΔvscF and complementation strain CΔvscF. Compared with those of wild-type POR-1 and CΔvscF, the cytotoxic, adherent, and apoptotic abilities of ΔvscF in HeLa cells were significantly reduced (P < 0.01). Furthermore, in infected HeLa cells, the mutant strain reduced the translocation rates of VP1683 and VP1686 effectors compared to the wild-type and complementation strains. A BLAST search showed that vscF is homologous to the MixH needle protein of Shigella flexneri, indicating that the vscF gene encodes the needle protein of T3SS1 in V. parahaemolyticus. Additional translocation assays showed that VPA0226 translocated into the HeLa eukaryotic cytoplasm via T3SS1, secretion assays showed that VPA0226 can be secreted to supernatant by T3SS1, indicating that VPA0226 belongs to the unpublished class of T3SS1 effectors. In conclusion, our data indicate an essential role of vscF in V. parahaemolyticus T3SS1 and revealed that VPA0226 can be secreted into the host cell cytoplasm via T3SS1. This study provides insights into a previously unexplored aspect of T3SS1, which is expected to contribute to the understanding of its infection mechanism.

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Helical structure of the needle of the type III secretion system of Shigella flexneri.

Cited by 3 publications

References 0 publications

The blueprint of the type-3 injectisome

The blueprint of the type-3 injectisome

Comparative transcriptomic analysis provides insights into transcription mechanisms of Vibrio parahaemolyticus T3SS during interaction with HeLa cells

VscF in T3SS1 Helps to Translocate VPA0226 in Vibrio parahaemolyticus

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