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Protein Membrane Overlay Assay: A Protocol to Test Interaction Between Soluble and Insoluble Proteins in vitro
Published on: August 14, 2011
Functional interaction between Cydia pomonella granulovirus IAP proteins
1Department of Biological Sciences, Imperial College of Science, Technology and Medicine, Imperial College Road, London SW7 2AZ, UK. lv@wpo.nerc.ac.uk
Virus Research
|February 28, 2003
Summary
Cydia pomonella granulovirus (CpGV) encodes three inhibitor of apoptosis (IAP) proteins. CpIAP5 enhances CpIAP3
Area of Science:
- Molecular biology
- Virology
- Insect pathology
Background:
- Baculoviruses encode inhibitor of apoptosis (IAP) proteins to regulate host cell death.
- Cydia pomonella granulovirus (CpGV) encodes three IAPs: CpIAP3, Cp94, and CpIAP5.
- CpIAP3 can substitute for the p35 gene in blocking Autographa californica nucleopolyhedrovirus (AcMNPV)-induced apoptosis.
Purpose of the Study:
- To investigate the functions of CpGV IAP proteins Cp94 and CpIAP5.
- To determine if Cp94 and CpIAP5 interact functionally with CpIAP3.
Main Methods:
- Transient expression experiments were performed.
- Apoptosis was induced using actinomycin D.
- The ability of CpGV IAPs to block apoptosis was assessed.
Main Results:
- Cp94 and CpIAP5, individually or together, did not block actinomycin D-induced apoptosis.
- CpIAP5 significantly enhanced the anti-apoptotic activity of CpIAP3.
- This study provides the first evidence of functional interactions between IAPs from a single baculovirus.
Conclusions:
- CpGV IAP proteins Cp94 and CpIAP5 have distinct functions.
- CpIAP5 plays a crucial role in modulating CpIAP3's anti-apoptotic activity.
- Functional interactions among baculoviral IAPs encoded by the same virus are possible.
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