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The baculovirus GP64 envelope fusion protein: synthesis, oligomerization, and processing
A G Oomens1, S A Monsma, G W Blissard
1Boyce Thompson Institute for Plant Research, Cornell University, Ithaca, New York 14853-1801, USA.
Virology
|June 1, 1995
Summary
Baculovirus GP64 envelope fusion protein (GP64 EFP) forms trimers rapidly but inefficiently. Carbohydrate processing slows down as baculovirus infection progresses.
Area of Science:
- Virology
- Molecular Biology
- Cell Biology
Background:
- Baculovirus GP64 envelope fusion protein (GP64 EFP) is crucial for viral entry.
- GP64 EFP follows the secretory pathway, undergoing oligomerization and processing.
- Understanding GP64 EFP's post-translational modifications is key to viral replication.
Purpose of the Study:
- To investigate the kinetics of GP64 EFP biosynthesis, oligomerization, and processing in infected cells.
- To determine the oligomeric structure of GP64 EFP.
- To analyze the efficiency and timing of GP64 EFP post-translational modifications throughout the infection cycle.
Main Methods:
- Pulse labeling and pulse-chase experiments to track protein synthesis and modification.
- Immunoprecipitation to isolate and identify GP64 EFP.
- Gel filtration chromatography, SDS-PAGE, and mass spectrometry to determine oligomeric structure.
Main Results:
- GP64 EFP synthesis peaks late in infection (24-26 hr post-infection).
- GP64 EFP forms homotrimers, but oligomerization is inefficient (<33% efficiency).
- Carbohydrate processing is rapid initially but becomes less efficient later in infection.
Conclusions:
- GP64 EFP forms homotrimeric structures through a rapid yet inefficient oligomerization process.
- Carbohydrate addition is fast, but processing is time-consuming and declines in efficiency during late infection.
- These findings shed light on the post-translational regulation of baculovirus fusion proteins.