A Deletion Variant Study of the Functional Role of the Salmonella Flagellin Hypervariable Domain Region in Motility

Malapaka, Raghu Ram V.; Adebayo, Leslie O.; Tripp, Brian C.

doi:10.1016/j.jmb.2006.10.054

Cited by 53 publications

(56 citation statements)

References 76 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The flagellar hook is extended by a long (up to 10 mm) semi-rigid helical filament made of flagellin; hook and filament are joined by two junction proteins. The C-and N-terminal domains of flagellins are conserved and allow the folding and polymerization into an 11 start helical tube, while the middle domain, exposed on the outer surface of the filament, varies between species [44].…”

Section: Structural and Functional Homologies Among The T3ss And Othementioning

confidence: 99%

Type III secretion systems: the bacterial flagellum and the injectisome

Diepold

Armitage

2015

Phil. Trans. R. Soc. B

189

175

View full text Add to dashboard Cite

One contribution of 12 to a theme issue 'The bacterial cell envelope'. The flagellum and the injectisome are two of the most complex and fascinating bacterial nanomachines. At their core, they share a type III secretion system (T3SS), a transmembrane export complex that forms the extracellular appendages, the flagellar filament and the injectisome needle. Recent advances, combining structural biology, cryo-electron tomography, molecular genetics, in vivo imaging, bioinformatics and biophysics, have greatly increased our understanding of the T3SS, especially the structure of its transmembrane and cytosolic components, the transcriptional, post-transcriptional and functional regulation and the remarkable adaptivity of the system. This review aims to integrate these new findings into our current knowledge of the evolution, function, regulation and dynamics of the T3SS, and to highlight commonalities and differences between the two systems, as well as their potential applications.

show abstract

Section: Structural and Functional Homologies Among The T3ss And Othementioning

confidence: 99%

Type III secretion systems: the bacterial flagellum and the injectisome

Diepold

Armitage

2015

Phil. Trans. R. Soc. B

189

175

View full text Add to dashboard Cite

show abstract

“…The central variable region of flagellin forms the outside surface-exposed domain (D2 and D3) in the assembled filament. Studies of the variable region have focused on its role in H antigenicity, the effect of deletions on filament formation and motility, and the insertion of foreign peptides for extracellular display on bacterial flagella (Malapaka et al, 2007;Reid et al, 1999;Westerlund-Wikström, 2000;Woodset al, 2007;Yoshioka et al, 1995). Thus, flagellin glycan structures are restricted in the D2 and D3 domains (a few glycans were located at the D2 proximal end of the D1 domain), and it is considered that these glycan moieties are exposed to environmental conditions ( Figure 3).…”

Section: Flagellin Glycosylationsmentioning

confidence: 99%

Flagellar Glycosylation: Current Advances

Hayakawa¹,

Ishizuka²

2012

Glycosylation

View full text Add to dashboard Cite

“…8 Flagellin contains two highly conserved N/C domains (D0 and D1) and one central hypervariable domain (D2/D3). [9][10][11] The hypervariable domain is vastly diverse in size and amino-acid composition among bacterial strains and species. 4 The conserved D0 and D1 domains are required for the immune activity of flagellin as a pathogen-associated molecular pattern.…”

Section: Introductionmentioning

confidence: 99%

Over-activation of TLR5 signaling by high-dose flagellin induces liver injury in mice

et al. 2014

View full text Add to dashboard Cite

Flagellin is a potent activator of a broad range of cell types that are involved in innate and adaptive immunity. Therefore, it is a good adjuvant candidate for vaccines, and it might function as a biological protectant against both major acute radiation syndrome during cancer radiotherapy and a mitigator of radiation emergencies. However, accumulating evidence has implicated flagellin in the occurrence of some inflammatory diseases, such as acute lung inflammation, cardiovascular collapse and inflammatory bowel disease. The aim of this study was to elucidate whether only flagellin-TLR5 signaling activation plays a role in the pathophysiology of liver or whether some other flagellin activity also contributes to liver injury either via bacterial infections or during clinical applications. Recombinant flagellin proteins with or without TLR5-stimulating activity were used to evaluate the role of flagellin-TLR5 signaling in liver injury in wild-type and TLR5 KO mice. Gross lesions and large areas of hepatocellular necrosis were observed in liver tissue 12 h after the intraperitoneal administration of 100 or 200 mg flagellin (FliC) in a dose-and time-dependent manner in wild-type mice, but not in TLR5 KO mice. Deletion of the N-terminal or TLR5 binding domain of flagellin inhibited flagellin-induced inflammatory responses and the subsequent acute liver function abnormality and damage. These data confirmed that flagellin is an essential determinant of liver injury and demonstrated that the over-activation of TLR5 signaling by high-dose flagellin caused acute inflammatory responses, neutrophil accumulation and oxidative stress in the liver, which contributes to the progression and severity of flagellin-induced liver injury.

show abstract

A Deletion Variant Study of the Functional Role of the Salmonella Flagellin Hypervariable Domain Region in Motility

Cited by 53 publications

References 76 publications

Type III secretion systems: the bacterial flagellum and the injectisome

Type III secretion systems: the bacterial flagellum and the injectisome

Flagellar Glycosylation: Current Advances

Over-activation of TLR5 signaling by high-dose flagellin induces liver injury in mice

Contact Info

Product

Resources

About