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Isolation of Cognate RNA-protein Complexes from Cells Using Oligonucleotide-directed Elution
Published on: January 16, 2017
A physical link between the pseudorabies virus capsid and the nuclear egress complex
Mindy Leelawong1, Dongsheng Guo, Gregory A Smith
1Department of Microbiology-Immunology, Northwestern University Feinberg School of Medicine, 303 E. Chicago Ave., Morton 3-603, Chicago, IL 60611, USA.
Journal of Virology
|September 2, 2011
Summary
The herpesvirus nuclear egress complex protein pUL31 binds to capsids only when pUL34 is absent. This conditional binding is crucial for targeting DNA-containing capsids during nuclear egress.
Area of Science:
- Virology
- Molecular Biology
- Cell Biology
Background:
- Herpesvirus capsids exit the nucleus via the inner nuclear membrane.
- This nuclear egress requires two conserved viral proteins: pUL31 and pUL34.
Purpose of the Study:
- To investigate the capsid-binding properties of the pUL31 protein.
- To determine the role of pUL34 in mediating the pUL31-capsid interaction.
Main Methods:
- Fluorescence microscopy to visualize protein-capsid interactions.
- Western blot analysis of purified intranuclear capsids.
- Testing interactions with viral proteins pUL25, pUL6, and pUL33.
Main Results:
- pUL31 is a conditional capsid-binding protein, unmasked in the absence of pUL34.
- The pUL31-capsid interaction was confirmed using microscopy and Western blot.
- None of the tested viral proteins (pUL25, pUL6, pUL33) were required for pUL31-capsid binding.
Conclusions:
- Provides the first evidence of a herpesvirus nuclear egress complex interacting with capsids.
- Suggests a mechanism for selective targeting of DNA-containing capsids for nuclear egress.
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