Secretory signal peptide modification for optimized antibody-fragment expression-secretion in Leishmania tarentolae.

ABSTRACT:

Background

Secretory signal peptides (SPs) are well-known sequence motifs targeting proteins for translocation across the endoplasmic reticulum membrane. After passing through the secretory pathway, most proteins are secreted to the environment. Here, we describe the modification of an expression vector containing the SP from secreted acid phosphatase 1 (SAP1) of Leishmania mexicana for optimized protein expression-secretion in the eukaryotic parasite Leishmania tarentolae with regard to recombinant antibody fragments. For experimental design the online tool SignalP was used, which predicts the presence and location of SPs and their cleavage sites in polypeptides. To evaluate the signal peptide cleavage site as well as changes of expression, SPs were N-terminally linked to single-c

SUBMITTER: Klatt S 

PROVIDER: S-EPMC3416730 | biostudies-literature | 2012 Jul

REPOSITORIES: biostudies-literature