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Hantavirus nucleocapsid protein oligomerization.
A Alfadhli1, Z Love, B Arvidson
1Vollum Institute and Department of Microbiology, Oregon Health Sciences University, Portland, Oregon 97201-3098, USA.
Journal of Virology
|February 13, 2001
Summary
Hantavirus nucleocapsid (N) protein oligomerization is crucial for virus assembly. This study reveals that N protein trimers, potentially formed by coiled-coil motifs, are key intermediates in hantavirus particle formation.
Area of Science:
- Virology
- Molecular Biology
- Structural Biology
Background:
- Hantaviruses are pathogenic RNA viruses causing severe human diseases.
- The nucleocapsid (N) protein is essential for hantavirus assembly, but its oligomerization mechanisms are unclear.
Purpose of the Study:
- To biochemically and genetically analyze the oligomerization of the hantavirus N protein.
- To investigate the role of N protein interactions in hantavirus particle assembly.
Main Methods:
- Bacterial expression and purification of N protein.
- Gradient fractionation and chemical cross-linking of viral particles.
- Yeast two-hybrid assays to study N protein interactions.
Main Results:
- Bacterially expressed N protein exists as dimers and trimers, in addition to larger aggregates.
- Cross-linking of viral particles suggests N protein trimers (140-150 kDa).
- Yeast two-hybrid analysis identified specific domains involved in N protein association, with N-terminal residues predicted to form trimeric coiled coils.
Conclusions:
- Coiled-coil motifs in the N-terminal region likely mediate N protein trimerization.
- Nucleocapsid protein trimers represent critical intermediates in the assembly of infectious hantavirus particles.