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. 2010 Jul 22;6(7):e1000943.
doi: 10.1371/journal.ppat.1000943.

RNA virus replication complexes

Yizhi Jane Tao  1 , Qiaozhen Ye
Affiliations

RNA virus replication complexes

Yizhi Jane Tao et al. PLoS Pathog. .
No abstract available

PubMed Disclaimer

Conflict of interest statement

The authors have declared that no competing interests exist.

Figures

Figure 1
Figure 1. RNA virus replication machineries.
(A) RdRps of hepatitis C virus and reovirus. Hepatitis C virus is a (+)RNA virus from the Flaviviridae family, while reovirus is a dsRNA virus belonging to the Reoviridae family. In both structures, the fingers, palm, and the thumb of the polymerase are colored in blue, red, and green, respectively. Yellow and magenta highlight the N- and C-terminal domains, respectively. The three aspartic acid residues in the polymerase catalytic active site are shown in cyan. Reovirus RdRP has large N- and C-terminal domains with distinct functions: the N-terminal domain maintains the closed conformation of the active site, and the C-terminal domain serves as a processivity factor like a sliding clamp. (B) The yeast L-A virus (Totiviridae family). The two independent sets of capsid protein molecules, 60 copies each, are shown in red and yellow, respectively. The viral RdRP is likely to be tethered to the inner capsid near the 5-fold symmetry axis, and viral transcripts made inside the core are released through channels on or near the 5-fold axes. (C) An influenza A virus (Orthomyxoviridae family) RNP model. Blue spheres represent NP monomers, and the green line shows vRNA. A short duplex formed between the 5′ and the 3′ ends provides the binding site for the heterotrimeric RdRp. Overall, the RNP assumes a rod-shaped, double-helical structure that remains intact even after the vRNA is removed.
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