Cryo-EM structure of the respiratory syncytial virus RNA polymerase.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 31953395.
- Also identified by DOI 10.1038/s41467-019-14246-3 and PMC identifier 6969064.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
The respiratory syncytial virus (RSV) RNA polymerase, constituted of a 250 kDa large (L) protein and tetrameric phosphoprotein (P), catalyzes three distinct enzymatic activities - nucleotide polymerization, cap addition, and cap methylation. How RSV L and P coordinate these activities is poorly understood. Here, we present a 3.67 Å cryo-EM structure of the RSV polymerase (L:P) complex. The structure reveals that the RNA dependent RNA polymerase (RdRp) and capping (Cap) domains of L interact with the oligomerization domain (P<sub>OD</sub>) and C-terminal domain (P<sub>CTD</sub>) of a tetramer of P. The density of the methyltransferase (MT) domain of L and the N-terminal domain of P (P<sub>NTD</sub>) is missing. Further analysis and comparison with other RNA polymerases at different stages suggest the structure we obtained is likely to be at an elongation-compatible stage. Together, these data provide enriched insights into the interrelationship, the inhibitors, and the evolutionary implications of the RSV polymerase.
Medical subject headings
- Cryoelectron Microscopy
- DNA-Directed RNA Polymerases
- RNA-Dependent RNA Polymerase
- Respiratory Syncytial Virus, Human
- Viral Proteins