Cryo-EM structure of the respiratory syncytial virus RNA polymerase

Dongdong Cao, Yunrong Gao, Claire Roesler, Samantha Rice, Paul D’Cunha, Lisa Zhuang, Julia Slack, Mason Domke, Anna Antonova, Sarah Romanelli, Shayon Keating, Gabriela Forero, Puneet Juneja and Bo Liang ()
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Dongdong Cao: Emory University School of Medicine
Yunrong Gao: Emory University School of Medicine
Claire Roesler: Emory University School of Medicine
Samantha Rice: Emory University School of Medicine
Paul D’Cunha: Emory University School of Medicine
Lisa Zhuang: Emory University School of Medicine
Julia Slack: Emory University School of Medicine
Mason Domke: Emory University School of Medicine
Anna Antonova: Emory University School of Medicine
Sarah Romanelli: Emory University School of Medicine
Shayon Keating: Emory University School of Medicine
Gabriela Forero: Emory University School of Medicine
Puneet Juneja: Emory University School of Medicine
Bo Liang: Emory University School of Medicine

Nature Communications, 2020, vol. 11, issue 1, 1-9

Abstract: 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 (POD) and C-terminal domain (PCTD) of a tetramer of P. The density of the methyltransferase (MT) domain of L and the N-terminal domain of P (PNTD) 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.

Date: 2020
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DOI: 10.1038/s41467-019-14246-3

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