%0 Journal Article
%@ 01681656
%A Bisht, Himani
%A Chugh, Dipti A
%A Raje, Manoj
%A Swaminathan, S
%A Khanna, Navin
%D 2002
%F open:901
%I Elsevier Science
%J Journal of Biotechnology
%K Dengueenvelopeprotein; HepatitisBsurfaceantigen; Pichiapastoris
%N 2
%P 97-110
%T Recombinant dengue virus type 2 envelope/hepatitis B surface antigen hybrid protein expressed in Pichia pastoris can function as a bivalent immunogen
%U http://crdd.osdd.net/open/901/
%V 99
%X A truncated version of the denguevirustype2envelopeprotein (Den2E) encoding the first 395 amino acid (aa) residues, and Den2E fused in-frame with the full-length 226-aa hepatitisBsurfaceantigen (Den2E-HBsAg) protein were expressed in the methylotrophic yeast, Pichiapastoris. Both the recombinantproteins showed evidence of the capacity to form high molecular weight aggregates. Electron microscopic analysis of the purified proteins showed that while Den2E displayed an amorphous morphology, Den2E-HBsAg existed as well-structured virus-like particles (VLPs). Using immuno-gold electron microscopy, these VLPs were demonstrated to contain both components of the Den2E-HBsAg hybridprotein. Seroanalysis showed that the hybrid VLPs could function in vivo as bivalent immunogens, which could elicit immune responses directed against both components of the hybridprotein, as evidenced by ELISA, immunoprecipitation and immunofluorescence data.
%Z Copyright of this article belongs to Elsevier Science.