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Cytoplasmic dynein LC8 interacts with lyssavirus phosphoprotein
Y Jacob1, H Badrane, P E Ceccaldi
1Laboratoire des Lyssavirus, Institut Pasteur, 75724 Paris Cedex 15, France. yjacob@pasteur.fr
Journal of Virology
|October 12, 2000
Summary
Rabies virus and Mokola virus phosphoproteins interact with dynein light chain LC8. This interaction suggests a common mechanism for lyssavirus transport within neurons and potential roles in pathogenesis.
Area of Science:
- Virology
- Cell Biology
- Neuroscience
Background:
- Cytoplasmic dynein light chain (LC8) is crucial for intracellular transport.
- Lyssaviruses, including rabies virus, cause significant neurological diseases.
Purpose of the Study:
- To investigate the interaction between lyssavirus phosphoproteins and host cell factors.
- To elucidate the role of these interactions in viral pathogenesis and transport.
Main Methods:
- Yeast two-hybrid screening of a human brain cDNA library.
- Confirmation using laser confocal microscopy and coimmunoprecipitation.
- Mapping of the interacting domain on the viral phosphoprotein.
Main Results:
- The cytoplasmic dynein light chain (LC8) was identified as interacting with the phosphoprotein (P) of rabies virus and Mokola virus.
- The interaction was confirmed through colocalization and coimmunoprecipitation experiments.
- The N-terminal half of the P protein (186 amino acids) was mapped as the dynein-binding domain.
Conclusions:
- The interaction between lyssavirus P proteins and dynein LC8 is likely a conserved mechanism across lyssaviruses, potentially facilitating viral nucleocapsid transport.
- This interaction may play a role in the pathogenesis of rabies virus by influencing cellular mechanisms like neuronal nitric oxide synthase inhibition.