Non-polar distribution of green fluorescent protein on the surface of Autographa californica nucleopolyhedrovirus using a heterologous membrane anchor

Heterogeneous proteins can be displayed on the surface of the budded form of Autographa californica nucleopolyhedrovirus (AcMNPV) after fusion of the display protein to the AcMNPV major envelope glycoprotein, gp64. However, display is restricted to the poles of the virion and is relatively low level...

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Bibliographic Details
Published in:Journal of biotechnology 2002-05, Vol.95 (3), p.269-275
Main Authors: Chapple, Susan D.J., Jones, Ian M.
Format: Article
Language:English
Subjects:
Baculovirus
Biological and medical sciences
Biotechnology
Expression vector
Fundamental and applied biological sciences. Psychology
Genetic engineering
Genetic technics
Genetic Vectors - genetics
Green Fluorescent Proteins
Luminescent Proteins - genetics
Luminescent Proteins - metabolism
Membrane incorporation
Methods. Procedures. Technologies
Nucleopolyhedrovirus - genetics
Nucleopolyhedrovirus - metabolism
Peptide Library
Recombinant Fusion Proteins - genetics
Surface display
Vectors (cloning, transfer, expression). Insertion sequences and transposons
Vesicular stomatitis Indiana virus - genetics
Viral Fusion Proteins - genetics
VSV G protein
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Summary:Heterogeneous proteins can be displayed on the surface of the budded form of Autographa californica nucleopolyhedrovirus (AcMNPV) after fusion of the display protein to the AcMNPV major envelope glycoprotein, gp64. However, display is restricted to the poles of the virion and is relatively low level. To investigate the use of alternative membrane anchor sequences that would be compatible with virus surface display, we have constructed a display vector containing the gp64 signal peptide and a membrane anchor from the vesicular stomatitis virus (VSV) G glycoprotein. Introduction of a gene encoding green fluorescent protein (GFP) between these signals led to abundant display of GFP on the surface of insect cells and on recombinant budded virions. In addition, and in contrast to gp64 based fusion proteins, GFP was localized to the lateral virion surfaces.
ISSN:0168-1656
1873-4863
DOI:10.1016/S0168-1656(02)00023-8