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Journal Articles Cell Year : 2019

Structure of the Respiratory Syncytial Virus Polymerase Complex

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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
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Dates and versions

hal-02353778 , version 1 (07-11-2019)

Identifiers

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