Andrea K. Vaags, Tessa N. Campbell, Francis Y.M. Choy
Published September 6, 2005
Genet. Mol. Res. 4 (3): 491-495 (2005)

About the Authors
Andrea K. Vaags, Tessa N. Campbell, Francis Y.M. Choy

Corresponding author
T.N. Campbell
Email: tcampb@ucalgary.ca

ABSTRACT. Gaucher disease, the most common lysosomal storage disorder, is currently treated with enzyme replacement therapy. This approach, however, is ineffective in altering the progression of neurodegeneration in type 2 and type 3 patients due to the difficulty of transferring the recombinant enzyme across the blood-brain barrier. Human immunodeficiency virus type 1 trans-activating transcriptional activator protein (HIV TAT) contains a protein transduction domain that can be added to a fusion protein partner to allow for transport of the partner across membranes. Consequently, we examined the creation, production, and secretion of fusion constructs containing glucocerebrosidase and either wild-type TAT or modified TAT in Sf9 cells. All three constructs exhibited successful expression, with wild-type TAT chimeras showing lower levels of expression than modified TAT chimeras.

Key words: HIV TAT, Glucocerebrosidase, Gaucher, Transduction, Protein expression.