The 20 kDa C-terminally truncated form of pertussis toxin subunit S1 secreted fromBacillus subtilis

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Expression of a C terminally truncated form of pertussis toxin S1 subunit effectively induces protection against pertussis toxin following DNA-based immunization.

Four plasmids encoding different C terminally and N terminally truncated pertussis toxin S1 subunits of Bordetella pertussis were constructed and tested for inducibility of protection against pertussis toxin in mice after DNA-based immunization. The region encoding an N-terminal 180-amino-acid fragment of the S1 subunit had the most potent ability to induce protective immunity.

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Membrane localization of the S1 subunit of pertussis toxin in Bordetella pertussis and implications for pertussis toxin secretion.

Pertussis toxin is secreted from Bordetella pertussis with the assistance of the Ptl transport system, a member of the type IV family of macromolecular transporters. The S1 subunit and the B oligomer combine to form the holotoxin prior to export from the bacterial cell, although the site of assembly is not known. To better understand the pathway of pertussis toxin assembly and secretion, we exa...

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Adenylate cyclase toxin-mediated delivery of the S1 subunit of pertussis toxin into mammalian cells.

The adenylate cyclase toxin (ACT) of Bordetella pertussis internalizes its catalytic domain into target cells. ACT can function as a tool for delivering foreign protein antigen moieties into immune effector cells to induce a cytotoxic T lymphocyte response. In this study, we replaced the catalytic domain of ACT with an enzymatically active protein moiety, the S1 (ADP-ribosyltransferase) subunit...

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sequence variation of the pertussis toxin s1 subunit encoding gene in the clinical isolates of bordetella pertussis in iran

results the results showed that all the strains had the dominant allele ptxs1a. there were differences between the alleles of the clinical strains and the vaccine strain. conclusions in recent years, a significant increase in the incidence of pertussis has been reported worldwide. our findings regarding the allelic shift of the ptxs1 gene are similar to those reported in many european and ameri...

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Recombinant Production of a Novel Fusion Protein: Listeriolysin O Fragment Fused to S1 Subunit Of Pertussis Toxin

Background: Some resources have suggested that genetically inactivated pertussis toxoid (PTs) bear a more protective effect than chemically inactivated products. This study aimed to produce new version of PT, by cloning an inactive pertussis toxin S1 subunit (PTS1) in a fusion form with N-terminal half of the listeriolysin O (LLO) pore-forming toxin. Methods: Deposited pdb structure file of the...

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ژورنال

عنوان ژورنال: FEMS Microbiology Letters

سال: 1991

ISSN: 0378-1097,1574-6968

DOI: 10.1111/j.1574-6968.1991.tb04515.x