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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:Syed Shams Yazdani  Ahmad Rushdi Shakri  Priyabrata Pattnaik  M. Moshahid A. Rizvi  Chetan E. Chitnis
Affiliation:(1) Malaria Research Group, International Centre for Genetic Engineering and Biotechnology (ICGEB), Aruna Asaf Ali Marg, New Delhi, 110067, India;(2) Defence Research & Development Establishment, Jhansi Road, Gwalior, 474 002, India;(3) Department of Biosciences, Jamia Millia Islamia, Jamia Nagar, New Delhi, 110025, India
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.
Keywords:Codon optimization  Duffy binding protein  Malaria vaccine  Recombinant Escherichia coli   Synthetic gene
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