Many Gram-negative bacteria pathogenic to plants and animals deploy the type III secretion system (T3SS) to inject virulence factors into their hosts. All bacteria that rely on the T3SS to cause infectious diseases in humans have developed antibiotic resistance. The T3SS is an attractive target for developing new antibiotics because it is essential in virulence, and part of its structural component is exposed on the bacterial surface. The structural component of the T3SS is the needle apparatus, which is assembled from over 20 different proteins and consists of a base, an extracellular needle, a tip, and a translocon. This review summarizes the current knowledge on the structure and assembly of the needle, tip, and translocon.
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http://dx.doi.org/10.1002/pro.3682 | DOI Listing |
Vet Res
November 2023
Jiangxi Engineering Laboratory for the Development and Utilization of Agricultural Microbial Resources, Nanchang, Jiangxi, China.
Nat Commun
September 2023
Departments of Ophthalmology and Physiology & Biophysics, University of California, Irvine, CA, USA.
Macrophages infected with Gram-negative bacteria expressing Type III secretion system (T3SS) activate the NLRC4 inflammasome, resulting in Gasdermin D (GSDMD)-dependent, but GSDME independent IL-1β secretion and pyroptosis. Here we examine inflammasome signaling in neutrophils infected with Pseudomonas aeruginosa strain PAO1 that expresses the T3SS effectors ExoS and ExoT. IL-1β secretion by neutrophils requires the T3SS needle and translocon proteins and GSDMD.
View Article and Find Full Text PDFmBio
October 2022
Department of Molecular Biology and Microbiology, Case Western Reserve Universitygrid.67105.35, Cleveland, Ohio, USA.
The type III secretion system (T3SS) is a syringe-like virulence factor that delivers bacterial proteins directly into the cytoplasm of host cells. An essential component of the system is the translocon, which creates a pore in the host cell membrane through which proteins are injected. In Pseudomonas aeruginosa, the translocation pore is formed by proteins PopB and PopD and attaches to the T3SS needle via the needle tip protein PcrV.
View Article and Find Full Text PDFJ Membr Biol
October 2022
Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, MA, 01003, USA.
Type III secretion (T3S) systems are complex bacterial structures used by many pathogens to inject proteins directly into the cytosol of the host cell. These secretion machines evolved from the bacterial flagella and they have been grouped into families by phylogenetic analysis. The T3S system is composed of more than 20 proteins grouped into five complexes: the cytosolic platform, the export apparatus, the basal body, the needle, and the translocon complex.
View Article and Find Full Text PDFBraz J Microbiol
March 2022
MOE Joint International Research Laboratory of Animal Health and Food Safety, College of Veterinary Medicine, Nanjing Agricultural University, Nanjing, 210095, China.
Vibrio parahaemolyticus is an important foodborne pathogenic bacterium that harbors the type III secretion system 1 (T3SS1) as an essential virulence factor. However, the pathogenesis and infection mechanism mediated by T3SS1 are not entirely clarified. Similar to previous studies on other T3SS-positive bacteria, the T3SS1 needle is a major extracellular component in V.
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