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Improvement in yield and purity of a recombinant malaria vaccine candidate based on the receptor-binding domain of Plasmodium vivax Duffy binding protein by codon optimization.

Authors
  • Yazdani, Syed Shams
  • Shakri, Ahmad Rushdi
  • Pattnaik, Priyabrata
  • Rizvi, M Moshahid A
  • Chitnis, Chetan E
Type
Published Article
Journal
Biotechnology letters
Publication Date
Jul 01, 2006
Volume
28
Issue
14
Pages
1109–1114
Identifiers
PMID: 16794771
Source
Medline
License
Unknown

Abstract

A recombinant blood-stage vaccine for Plasmodium vivax malaria based on the functional receptor-binding domain of PvDBP (PvRII) has been developed. A synthetic gene coding for PvRII was expressed in Escherichia coli using codon optimization. Expression level of recombinant PvRII was 10% of the total cellular proteins. Truncated PvRII products, seen when the native PvRII gene was expressed, were absent in case of synthetic gene.

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