Cytotoxin with a subtilase domain

Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues

Reexamination Certificate

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Reexamination Certificate

active

07078489

ABSTRACT:
A member of a new class of bacterial toxin has been isolated and characterised. The bacterial toxin is of the AB5type and is characterised in that it has a subtilase domain. It is cytotoxic to Vero cells, and toxicity in vivo in mice occurs in a number of different sites. Mutation of the serine active residue results in greater than 99% reduction in activity. The protein has been purified and antibodies have been prepared for both the A subunit and B subunits, and ELISA detection methods have been developed. The nucleic acid sequence has been determined and primers specific for the toxin have been used for a preliminary screen of a range of patient samples to ascertain the extent to which the toxin is present.

REFERENCES:
Patton et al. 2001; Characterization of Saa, a Novel Autoagglutinating Adhesion Produced by Locus of Enterocyte Effacement-Negative Shiga-ToxigenicEscherichia coliStrains That Are Virulent for Humans. Infection and Immunity 69(11): 6999-7009.
Srimanote et al. 2002; Characterization of a Novel Type IV Pilus Locus Encoded on the Larg Plasmid of Locus of Enterocyte Effacement-Negative Shiga-ToxigenicEscherichia coliStrains That Are Virulent for Humans. Infection and Immunity, 70(6): 3094-3100.
Paton et al. 2004; A New Family of Potent AB5 Cytotoxins Produced by Shiga ToxigenicEscherichia coli. J. Exp. Med. 200(1): 35-46.

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