scholarly journals Study of the immunogenicity of the VP2 protein of canine parvovirus produced using an improved Baculovirus expression system

2020 ◽  
Vol 16 (1) ◽  
Author(s):  
Dao Chang ◽  
Yangkun Liu ◽  
Yangyang Chen ◽  
Xiaomin Hu ◽  
Andrey Burov ◽  
...  
Keyword(s):  
Expression System ◽  
Baculovirus Expression System ◽  
Canine Parvovirus ◽  
Vp2 Protein ◽  
Baculovirus Expression

Production of VP2 protein of canine parvovirus-2c expressed in baculovirus expression system

2020 ◽  
Vol 44 (2) ◽  
pp. 96-98
Author(s):  
Seyeon Park ◽  
◽  
Ju-Yeon Lee ◽  
Jae Young Song ◽  
Yoon-Hee Lee ◽  
...  
Keyword(s):  
Expression System ◽  
Baculovirus Expression System ◽  
Canine Parvovirus ◽  
Vp2 Protein ◽  
Baculovirus Expression

scholarly journals Enhanced production of Canine parvovirus VP2  protein using improved Baculovirus expression  system  and its immunogenicity

2020 ◽  
Author(s):  
Dao Chang ◽  
Yangkun Liu ◽  
Yangyang Chen ◽  
Xiaomin Hu ◽  
Andrey Burov ◽  
...  
Keyword(s):  
Expression System ◽  
Baculovirus Expression System ◽  
Canine Parvovirus ◽  
Full Length ◽  
Recombinant Viruses ◽  
Vp2 Protein ◽  
Enhanced Production ◽  
Baculovirus Expression ◽  
Yield Production ◽  
High Level

Abstract Background : Canine parvovirus (CPV) is now recognized as a serious threat to dog industry worldwide. Vaccination remains the principal tool to control CPV infection. However, due to low yield, production of VP2 protein of CPV in baculovirus expression system remains challenging. The aim of this study was to increase the VP2 protein production by using a improved baculovirus expression system (Multibac) and evaluate the immunogenicity of the purified VP2 protein in mice. Results: The results showed that CPV VP2 protein was successfully expressed in the improved baculovirus expression system efficiently. A high level of expression of the full length VP2 protein was achieved using our modified system. The recombinant virus carrying two copies of VP2 showed the highest expression level, with a productivity of 186 mg/L, which is about 1.4-1.6 fold that of the recombinant viruses carrying only one copy. The purified protein could react with Mouse anti-His tag monoclonal antibody and Rabbit anti-VP2 polyclonal antibody with good reactogenicity. The mice were then immunized with purified full length VP2 protein to evaluate its immunogenicity. After vaccination, VP2 protein could induce the mice produce high level of hemagglutination inhibition antibodies. Conclusions: Full length CPV VP2 protein was successfully expressed at high level and purified efficiently. And it stimulated mice to produce high level of antibody. The full length VP2 expressed in this study could be used as a putative economic and efficient subunit vaccine against CPV infection.

Production of recombinant new canine parvovirus 2a viral protein 2 in SF9 cells using a baculovirus expression system

2020 ◽  
Vol 44 (3) ◽  
pp. 142-145
Author(s):  
Hyeonhae Choi ◽  
Seyeon Park ◽  
Yoon-Hee Lee ◽  
Ju-Yeon Lee ◽  
Jae Young Song ◽  
...  
Keyword(s):  
Viral Protein ◽  
Expression System ◽  
Baculovirus Expression System ◽  
Canine Parvovirus ◽  
Sf9 Cells ◽  
Baculovirus Expression

scholarly journals Expression of functional G protein beta gamma dimers of defined subunit composition using a baculovirus expression system.

1992 ◽  
Vol 267 (19) ◽  
pp. 13123-13126 ◽  
Author(s):  
S.G. Graber ◽  
R.A. Figler ◽  
V.K. Kalman-Maltese ◽  
J.D. Robishaw ◽  
J.C. Garrison
Keyword(s):  
G Protein ◽  
Expression System ◽  
Baculovirus Expression System ◽  
Subunit Composition ◽  
Baculovirus Expression

scholarly journals Production, processing and partial purification of functional G protein βγ subunits in baculovirus-infected insect cells

1992 ◽  
Vol 286 (3) ◽  
pp. 677-680 ◽  
Author(s):  
J D Robishaw ◽  
V K Kalman ◽  
K L Proulx
Keyword(s):  
G Protein ◽  
G Proteins ◽  
Insect Cells ◽  
Expression System ◽  
Baculovirus Expression System ◽  
Partial Purification ◽  
Baculovirus Expression ◽  
Gamma Subunits ◽  
Infected Insect ◽  
Beta 2

As a result of the inability to resolve the heterogeneous mixture of G protein beta gamma subunits present in tissues, it has not been possible to compare different beta gamma subunits of the G proteins in terms of their proposed roles in receptor-effector coupling. This study was undertaken to establish the utility of the baculovirus expression system in producing homogeneous beta gamma subunits of defined composition for the comparative analysis of these subunits in reconstitution systems. In this study we report the expression, and appropriate post-translational processing, of recombinant beta 2, gamma 2 and gamma 3 subunits. In addition, we show that the recombinant beta gamma subunits can be readily purified, and can functionally interact with the alpha subunits of the G proteins.

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