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Background  Chicken anemia virus (CAV), the causative agent chicken anemia, is the only member of the genus  Gyrovirus  of the  Circoviridae  family. CAV is an immune suppressive virus and causes anemia, lymph organ atrophy and immunodeficiency. The production and biochemical characterization of VP1 protein and its use in a subunit vaccine or as part of a diagnostic kit would be useful to CAV infection prevention.    Results  Significantly increased expression of the recombinant full-length VP1 capsid protein from chicken anemia virus was demonstrated using an  E. coli  expression system. The VP1 gene was cloned into various different expression vectors and then these were expressed in a number of different  E. coli  strains. The expression of CAV VP1 in  E. coli  was significantly increased when VP1 was fused with GST protein rather than a His-tag. By optimizing the various rare amino acid codons within the N-terminus of the VP1 protein, the expression level of the VP1 protein in  E. coli  BL21(DE3)-pLysS was further increased significantly. The highest protein expression level obtained was 17.5 g/L per liter of bacterial culture after induction with 0.1 mM IPTG for 2 h. After purification by GST affinity chromatography, the purified full-length VP1 protein produced in this way was demonstrated to have good antigenicity and was able to be recognized by CAV-positive chicken serum in an ELISA assay.    Conclusions  Purified recombinant VP1 protein with the gene's codons optimized in the N-terminal region has potential as chimeric protein that, when expressed in  E. coli , may be useful in the future for the development of subunit vaccines and diagnostic tests.

High yield expression in a recombinant E. coli of a codon optimized chicken anemia virus capsid protein VP1 useful for vaccine development