Cloning, Expression and Purification of Clostridium botulinum Neurotoxin Type E Binding Domain

Immunogenic and Protective Potentials of Recombinant Receptor Binding Domain and a C-Terminal Fragment of Clostridium botulinum Neurotoxin Type E

Clostridium Botulinum Type E neurotoxin heavy chain consists of two domains: the translocation domain asthe N-terminal half and the binding domain as the Cterminal half (Hc). One effective way to neutralize botulinum neurotoxin is to inhibit binding of this toxin to neuromuscular synapses with antibodies against binding domain. Two synthetic genes, coding for Hc (the full length binding d...

Purification of Clostridium botulinum type A neurotoxin.

Expression and Purification of Neurotoxin-Associated Protein HA-33/A from Clostridium botulinum and Evaluation of Its Antigenicity

Background: Botulinum neurotoxin (BoNT) complexes consist of neurotoxin and neurotoxin-associated proteins. Hemagglutinin-33 (HA-33) is a member of BoNT type A (BoNT/A) complex. Considering the protective role of HA-33 in preservation of BoNT/A in gastrointestinal harsh conditions and also its adjuvant role, recombinant production of this protein is favorable. Thus in this study, HA-33 was expr...

Cloning of Binding Domain of Clostridium botlllinum Toxin Type A in Escherichia coli

The effect of pH on recombinant C-terminal domain of Botulinum Neurotoxin type E (rBoNT/E-HCC)

Recombinant proteins are tending to be the most favorable vaccine-candidates against botulism. Recombinant Carboxy-terminal of botulinum neurotoxin serotype E (rBoNT/E-HCC) has been introduced as an efficient vaccine against botulism type E. In this report, we made an effort to investigate the effect of different pH on protein structure to assess if rBoNT/E-HCC could be used as a vaccine for or...

Purification and activation of Clostridium botulinum type E toxin.

Type E strains of Clostridium botulinum tend to produce toxin of relatively low mouse killing power (administered intraperitoneally) in relation to its high lethality per os for man. The explanation of this peculiarity seems to lie in the phenomenon of "activation," whereby type E toxin, when exposed at an appropriate pH in vitro to certain bacterial enzymes (Dolman, 1953, 1957a; Sakaguchi and ...