Cloning and expression of a toxin-associated protein from Clostridium botulinum serotype E
Poster Number
21
Format
Poster Presentation
Abstract/Artist Statement
Clostridium botulinum, the agent of botulism, infects several individuals each year as it raises concerns regarding bioterrorism and food safety. Current antitoxins can treat botulism’s toxic effects, but prevention is preferable. This can be achieved through a sensitive and accurate detection of the toxin and/or its accessory proteins in food. To support this effort, botulism accessory proteins were recombinantly expressed and purified to generate monoclonal antibodies which may serve as probes for detecting the toxin. We cloned by PCR one such accessory protein, called p48, from C. botulinum serotype E. We first ligated the PCR product into the PCR 2.1 and then into the expression vector PQE80. Regulated expression was analyzed and confirmed via western blotting prior to protein purification.
Location
DeRosa University Center, Ballroom B
Start Date
2-5-2009 1:00 PM
End Date
2-5-2009 3:00 PM
Cloning and expression of a toxin-associated protein from Clostridium botulinum serotype E
DeRosa University Center, Ballroom B
Clostridium botulinum, the agent of botulism, infects several individuals each year as it raises concerns regarding bioterrorism and food safety. Current antitoxins can treat botulism’s toxic effects, but prevention is preferable. This can be achieved through a sensitive and accurate detection of the toxin and/or its accessory proteins in food. To support this effort, botulism accessory proteins were recombinantly expressed and purified to generate monoclonal antibodies which may serve as probes for detecting the toxin. We cloned by PCR one such accessory protein, called p48, from C. botulinum serotype E. We first ligated the PCR product into the PCR 2.1 and then into the expression vector PQE80. Regulated expression was analyzed and confirmed via western blotting prior to protein purification.