EXPRESSION OF A BIOACTIVE FUSION PROTEIN OF Escherichia coli HEAT- LABILE TOXIN B SUBUNIT TO A SYNAPSIN PEPTIDE

SCERBO MJ, BIBOLINI MJ, BARRA JL, ROTH GA, MONFERRAN CG

Elsevier

Año: 2008 vol. 59 p. 320 - 320

p class="MsoNormal" style="MARGIN: 0cm 0cm 0pt; LINE-HEIGHT: 200%">The B subunit of Escherichia coli heat labile toxin (LTB) may function as an efficient carrier molecule for the delivery of genetically coupled antigens across the mucosal barrier. We constructed vectors for the expression of LTB and LTBSC proteins. LTBSC is a fusion protein that comprises the amino acid sequence from the C-domain of rat synapsin fused to the C-terminal end of LTB. Both constructions have a coding sequence for a 6His-tag fused in-frame. LTBSC was expressed in Escherichia coli as inclusion bodies. The inclusion bodies were isolated and purified by Ni2+-chelating affinity chromatography under denaturing condition. Purified LTBSC