Skip to Main content Skip to Navigation
Journal articles

Structure of the Respiratory Syncytial Virus Polymerase Complex

Abstract : Graphical Abstract Highlights d Cryo-EM structure of RSV L bound by tetrameric RSV P solved to 3.2 Å d P tetramer adopts an asymmetric tentacular arrangement when bound to L d L priming loop adopts elongation-compatible state without PRNTase-RdRp separation d Structure rationalizes escape from small-molecule antivirals In Brief Respiratory syncytial virus (RSV) remains a leading cause of bronchiolitis and hospitalization, especially of infants. Gilman et al. present a 3.2-Å cryo-EM structure of the RSV L polymerase in complex with the P phosphoprotein-components of the core viral replication machinery that represent an attractive target for the development of therapeutic agents. Data Resources 6PZK
Complete list of metadatas

Cited literature [93 references]  Display  Hide  Download

https://hal-amu.archives-ouvertes.fr/hal-02353778
Contributor : Etienne Decroly <>
Submitted on : Thursday, November 7, 2019 - 2:26:45 PM
Last modification on : Monday, July 6, 2020 - 1:28:03 PM
Long-term archiving on: : Sunday, February 9, 2020 - 12:07:04 AM

File

PIIS009286741930902X.pdf
Files produced by the author(s)

Identifiers

Collections

Citation

Morgan Gilman, Cheng Liu, Amy Fung, Ishani Behera, Paul Jordan, et al.. Structure of the Respiratory Syncytial Virus Polymerase Complex. Cell, Elsevier, 2019, 179 (1), pp.193-204.e14. ⟨10.1016/j.cell.2019.08.014⟩. ⟨hal-02353778⟩

Share

Metrics

Record views

190

Files downloads

256