Optimizing expression of the pregnancy malaria vaccine candidate, VAR2CSA in Pichia pastoris.

ABSTRACT:

Background

VAR2CSA is the main candidate for a vaccine against pregnancy-associated malaria, but vaccine development is complicated by the large size and complex disulfide bonding pattern of the protein. Recent X-ray crystallographic information suggests that domain boundaries of VAR2CSA Duffy binding-like (DBL) domains may be larger than previously predicted and include two additional cysteine residues. This study investigated whether longer constructs would improve VAR2CSA recombinant protein secretion from Pichia pastoris and if domain boundaries were applicable across different VAR2CSA alleles.

Methods

VAR2CSA sequences were bioinformatically analysed to identify the predicted C11 and C12 cysteine residues at the C-termini of DBL domains and revised N- and C-termimal dom

SUBMITTER: Avril M 

PROVIDER: S-EPMC2714522 | biostudies-literature | 2009 Jun

REPOSITORIES: biostudies-literature