Resistance of hemagglutinin-33, the type a botulinum neurotoxin associated protein to lysosomal proteases

BIOL 163

Shuowei Cai, scai@umassd.edu, Department of Chemistry and Biochemistry, University of Massachusetts Dartmouth, North Dartmouth, MA 02747
Clostridium botulinum, the agent responsible for the deadly food poisoning botulism disease, produces the most toxic protein, botulinum neurotoxin, known to the mankind. All of the serotypes (A-G) of BoNT secreted from the bacteria are not in free form but in a complex form along with one or more neurotoxin associated proteins (NAPs), which play a protective role against adversarial environmental conditions such as heat or acidity and proteases in the gastrointestinal tract. In case of type A C. botulinum, a 33 kDa protein that accounts for the largest proportion among the NAPs, referred to as Hn-33, was found to be resistant to protease digestion such as trypsin. We have now discovered a novel role of Hn-33, resistant to Cathepsin D, L, lysosomal proteases. This finding suggests that resistance of Hn-33 to lysosomal proteases may influence its biological action. The work was supported by a DoD/Army Contract No. W911NF-06-1-0095.
 

Frontiers in Chemical Biology
5:00 PM-7:00 PM, Wednesday, August 22, 2007 BCEC -- Exhibit Hall - B2, Poster

Division of Biological Chemistry

The 234th ACS National Meeting, Boston, MA, August 19-23, 2007