Journal
JOURNAL OF VIROLOGY
Volume 82, Issue 2, Pages 674-682Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.00935-07
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Funding
- NIAID NIH HHS [R01 AI050066, R56 AI050066, AI050066] Funding Source: Medline
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R56AI050066, R01AI050066] Funding Source: NIH RePORTER
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The crystal structure of the vesicular stomatitis virus nucleoprotein (N) in complex with RNA reveals extensive and specific intermolecular interactions among the N molecules in the 10-member oligomer. What roles these interactions play in encapsidating RNA was studied by mutagenesis of the N protein. Three N mutants intended for disruption of the intermolecular interactions were designed and coexpressed with the phosphoprotein (P) in an Escherichia coli system previously described (T.J. Green et al., J. Virol. 74:9515-9524, 2000). Mutants N (Delta 1-22), N (Delta 347-352), and N (320-324, (Ala)(5)) lost RNA encapsidation and oligomerization but still bound with P. Another mutant, N (Ser290 -> Trp), was able to form a stable ring-like N oligomer and bind with the P protein but was no longer able to encapsidate RNA. The crystal structure of N (Ser290 -> Trp) at 2.8 angstrom resolution showed that this mutant can maintain all the same intermolecular interactions as the wild-type N except for a slight unwinding of the N-terminal lobe. These results suggest that the intermolecular contacts among the N molecules are required for encapsidation of the viral RNA.
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