Fine mapping and characterization of the L-polymerase-binding domain of the respiratory syncytial virus phosphoprotein.

ABSTRACT:

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The minimum requirement for an active RNA-dependent RNA polymerase of respiratory syncytial virus (RSV) is a complex made of two viral proteins, the polymerase large protein (L) and the phosphoprotein (P). Here we have investigated the domain on P that is responsible for this critical P-L interaction. By use of recombinant proteins and serial deletions, an L binding site was mapped in the C-terminal region of P, just upstream of the N-RNA binding site. The role of this molecular recognition element of about 30 amino acid residues in the L-P interaction and RNA polymerase activity was evaluated in cellula using an RSV minigenome system and site-directed mutagenesis. The results highlighted the critical role of hydrophobic residues located in this region.

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SUBMITTER: Sourimant J 

PROVIDER: S-EPMC4442346 | biostudies-literature | 2015 Apr

REPOSITORIES: biostudies-literature