Properties of pertussis toxin B oligomer assembled in vitro from recombinant polypeptides produced by Escherichia coli

Burnette, W N; Arciniega, Juan; Mar, V L; Burns, Drusilla L

doi:10.1128/iai.60.6.2252-2256.1992

Cited by 10 publications

(6 citation statements)

References 39 publications

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“…The periplasmic disulfide bond‐catalyzing proteins DsbA‐C and reduced glutathione disulfides are required for efficient PTX assembly [18,19]. Holotoxin assembly takes place in the periplasm even in the absence of the Ptl machinery, as shown by studies conducted both in vivo and in vitro [20–23]. In the absence of S1, the B oligomer can also self assemble in the periplasm, although there have been conflicting reports in the literature [20,24].…”

Section: Biogenesis Of Ptxmentioning

confidence: 99%

The ins and outs of pertussis toxin

2011

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Pertussis toxin, produced and secreted by the whooping cough agent Bordetella pertussis, is one of the most complex soluble bacterial proteins. It is actively secreted through the B. pertussis cell envelope by the Ptl secretion system, a member of the widespread type IV secretion systems. The toxin is composed of five subunits (named S1 to S5 according to their decreasing molecular weights) arranged in an A-B structure. The A protomer is composed of the enzymatically active S1 subunit, which catalyzes ADP-ribosylation of the a subunit of trimeric G proteins, thereby disturbing the metabolic functions of the target cells, leading to a variety of biological activities. The B oligomer is composed of 1S2:1S3:2S4:1S5 and is responsible for binding of the toxin to the target cell receptors and for intracellular trafficking via receptor-mediated endocytosis and retrograde transport. The toxin is one of the most important virulence factors of B. pertussis and is a component of all current vaccines against whooping cough.

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Section: Biogenesis Of Ptxmentioning

confidence: 99%

The ins and outs of pertussis toxin

2011

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“…Initial attempts to express the subunits in E. coli were unsuccessful, probably due to decreased recognition of the PT promoter in E. coli (91,110). Substitution of the putative PT promoter with an E. coli promoter (tac or lac) allowed the expression of the individual subunits in E. coli (12,14,16,90). The gene for each subunit of PT encodes a signal sequence at the amino terminus which is cleaved upon export (91,109).…”

Section: Ptmentioning

confidence: 99%

The family of bacterial ADP-ribosylating exotoxins

1995

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Pathogenic bacteria utilize a variety of virulence factors that contribute to the clinical manifestation of their pathogenesis. Bacterial ADP-ribosylating exotoxins (bAREs) represent one family of virulence factors that exert their toxic effects by transferring the ADP-ribose moiety of NAD onto specific eucaryotic target proteins. The observations that some bAREs ADP-ribosylate eucaryotic proteins that regulate signal transduction, like the heterotrimeric GTP-binding proteins and the low-molecular-weight GTP-binding proteins, has extended interest in bAREs beyond the bacteriology laboratory. Molecular studies have shown that bAREs possess little primary amino acid homology and have diverse quaternary structure-function organization. Underlying this apparent diversity, biochemical and crystallographic studies have shown that several bAREs have conserved active-site structures and possess a conserved glutamic acid within their active sites.

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“…Recombinant pertussis toxin subunits have also been expressed and purified separately to form oligomers in vitro. They bear the potential to form in vitro assemblies, which are antigenic, and the antibodies they provoke have been displayed to have inhibitory activities against pertussis toxin [35] .…”

Section: Discussionmentioning

confidence: 99%

“…J. 25 (1): [33][34][35][36][37][38][39][40] and sufficient for a pertussis vaccine [9] . Moreover, a former study reported that fimbria, similar to pertactin, is unnecessary for vaccine-induced immunostimulation [10] .…”

Section: Introductionmentioning

confidence: 99%