منابع مشابه
Baculovirus surface display of Theileria parva p67 antigen preserves the conformation of sporozoite-neutralizing epitopes.
Theileria parva is an intracellular protozoan parasite that causes East Coast fever, a severe lymphoproliferative disease in cattle. Previous attempts to produce recombinant sporozoite surface antigen (p67) in bacterial or insect cells for vaccine purposes have not resulted in a correctly folded protein. Here, we report the expression of N- and C-terminal domains of p67 fused to the baculovirus...
متن کاملUse of hr 3 enhancer and P 74 TM domain in baculovirus surface display
1 The Key Laboratory of Cell Proliferation and Differentiation of Ministry of Education and The State Key Laboratory of Biomembrane and Membrane Bio-engineering, College of Life Sciences, Peking University, Beijing 100871, P. R. China, The Center for Theoretical Biology, Peking University, Beijing 100871, P. R. China, Institute of Virology, Zhejiang Provincial Center For Disease Prevention and ...
متن کاملBaculovirus surface display: construction and screening of a eukaryotic epitope library.
The baculovirus expression system was utilized to serve as a tool for ligand selection, demonstrating the applicability of the system to the generation and screening of eukaryotic expression libraries. The HIV-1-gp41 epitope 'ELDKWA', specific for the neutralizing human mAb 2F5, was inserted into the antigenic site B of influenza virus hemagglutinin and expressed on the surface of baculovirus i...
متن کاملSafety and Immunogenicity of H5N1 Influenza Vaccine Based on Baculovirus Surface Display System of Bombyx mori
Avian influenza virus (H5N1) has caused serious infections in human beings. This virus has the potential to emerge as a pandemic threat in humans. Effective vaccines against H5N1 virus are needed. A recombinant Bombyx mori baculovirus, Bmg64HA, was constructed for the expression of HA protein of H5N1 influenza virus displaying on the viral envelope surface. The HA protein accounted for approxim...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 2000
ISSN: 0014-2956
DOI: 10.1046/j.1432-1327.2000.01439.x