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Antheraea mylitta cytoplasmic polyhedrosis virus is a segmented dsRNA virus of the family Reoviridae. Segment 2 (S2)-encoded RNA-dependent RNA polymerase (RdRp) helps the virus to propagate its genome in the host cell of the silkworm, Antheraea mylitta. Cloning, expression, purification and functional analysis of individual domains of RdRp have demonstrated that the purified domains interact in vitro. The central polymerase domain (PD) shows nucleotide binding properties, but neither the N-terminal domain (NTD) nor the C-terminal domain (CTD). Isolated PD does not exhibit RdRp activity but this activity can be reconstituted when all three domains are included in the reaction mixture. Molecular dynamics simulation suggests that the isolated PD has increased internal motions in comparison to when it is associated with the NTD and CTD. The motions of the separated PD may lead to the formation of a less accessible RNA template-binding channel and, thus, impair RdRp activity.

Original publication

DOI

10.1099/jgv.0.000463

Type

Journal article

Journal

J Gen Virol

Publication Date

07/2016

Volume

97

Pages

1709 - 1719

Keywords

Amino Acid Sequence, Animals, Cloning, Molecular, Genome, Viral, Molecular Dynamics Simulation, Moths, Protein Structure, Tertiary, RNA Replicase, RNA, Viral, Reoviridae, Virus Replication