نتایج جستجو برای: letal toxin b

تعداد نتایج: 942877  

Journal: :Applied and environmental microbiology 1998
M A Andersson R Mikkola J Helin M C Andersson M Salkinoja-Salonen

Of the toxins produced by Bacillus cereus, the emetic toxin is likely the most dangerous but, due to the lack of a suitable assay, the least well known. In this paper, a new, sensitive, inexpensive, and rapid bioassay for detection of the emetic toxin of B. cereus is described. The assay is based on the loss of motility of boar spermatozoa upon 24 h of exposure to extracts of emetic B. cereus s...

2014
Lisa M. Russo Angela R. Melton-Celsa Michael J. Smith Alison D. O'Brien

Shiga toxin (Stx)-producing E. coli (STEC) cause food-borne outbreaks of hemorrhagic colitis. The main virulence factor expressed by STEC, Stx, is an AB5 toxin that has two antigenically distinct forms, Stx1a and Stx2a. Although Stx1a and Stx2a bind to the same receptor, globotriaosylceramide (Gb3), Stx2a is more potent than Stx1a in mice, whereas Stx1a is more cytotoxic than Stx2a in cell cult...

2003
SOLOMON KADIS ANNE V. TRENCHARD SAMUEL J. AJL

The solubility of the homogeneous, nonenzymatic structural protein isolated and purified from bovine heart mitochondria when incubated with the murine toxin of Pasteurella pesfis at pH 11.0 increases as the concentration of the toxin is increased. This indicates that a protein-protein interaction occurs between the monomeric units of the structural protein and the toxin. This interaction result...

Journal: :The Journal of biological chemistry 1966
S Kadis A V Trenchard S J Ajl

The solubility of the homogeneous, nonenzymatic structural protein isolated and purified from bovine heart mitochondria when incubated with the murine toxin of Pasteurella pesfis at pH 11.0 increases as the concentration of the toxin is increased. This indicates that a protein-protein interaction occurs between the monomeric units of the structural protein and the toxin. This interaction result...

Journal: :Infection and immunity 1987
M J Mitchell B E Laughon S Lin

We describe a simplified procedure for purification of Clostridium difficile toxin B. In this procedure, cytotoxicity is associated with a single protein band with a molecular mass of 230 kilodaltons. We used direct fluorescent staining of actin filaments to study the effect of this toxin on cultured cells. Morphologic changes were preceded by a decrease in the number and length of stress fiber...

Journal: :Infection and immunity 2000
K M Farizo T Huang D L Burns

We examined the structural components of pertussis toxin that are required for efficient export from Bordetella pertussis via the Ptl system, a member of the type IV family of macromolecular transporters. First, we constructed a strain of B. pertussis that contains a functional Ptl system but does not produce pertussis toxin. Plasmids which express either the S1 subunit or the B oligomer were t...

Journal: :Journal of cell science 2007
Vincent Popoff Gonzalo A Mardones Danièle Tenza Raúl Rojas Christophe Lamaze Juan S Bonifacino Graça Raposo Ludger Johannes

Previous studies have indicated a role for clathrin, the clathrin adaptors AP1 and epsinR, and the retromer complex in retrograde sorting from early/recycling endosomes to the trans Golgi network (TGN). However, it has remained unclear whether these protein machineries function on the same or parallel pathways. We show here that clathrin and the retromer subunit Vps26 colocalize at the ultrastr...

Journal: :The Journal of biological chemistry 2009
Martina Egerer Torsten Giesemann Christian Herrmann Klaus Aktories

Clostridium difficile toxins A and B are major virulence factors responsible for induction of pseudomembranous colitis and antibiotic-associated diarrhea in men. The toxins possess a multidomain structure and only the N-terminal glucosyltransferase domain, which inactivates Rho GTPases by glucosylation, is translocated into the cytosol of target cells. Processing of the toxin occurs by autocata...

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