Structures of the promoter-bound respiratory syncytial virus polymerase

Dongdong Cao, Yunrong Gao, Zhenhang Chen, Inesh Gooneratne, Claire Roesler, Cristopher Mera, Paul D’Cunha, Anna Antonova, Deepak Katta, Sarah Romanelli, Qi Wang, Samantha Rice, Wesley Lemons, Anita Ramanathan and Bo Liang ()
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Dongdong Cao: Emory University School of Medicine
Yunrong Gao: Emory University School of Medicine
Zhenhang Chen: Emory University School of Medicine
Inesh Gooneratne: Emory University School of Medicine
Claire Roesler: Emory University School of Medicine
Cristopher Mera: Emory University School of Medicine
Paul D’Cunha: Emory University School of Medicine
Anna Antonova: Emory University School of Medicine
Deepak Katta: Emory University School of Medicine
Sarah Romanelli: Emory University School of Medicine
Qi Wang: Emory University School of Medicine
Samantha Rice: Emory University School of Medicine
Wesley Lemons: Emory University School of Medicine
Anita Ramanathan: Emory University School of Medicine
Bo Liang: Emory University School of Medicine

Nature, 2024, vol. 625, issue 7995, 611-617

Abstract: Abstract The respiratory syncytial virus (RSV) polymerase is a multifunctional RNA-dependent RNA polymerase composed of the large (L) protein and the phosphoprotein (P). It transcribes the RNA genome into ten viral mRNAs and replicates full-length viral genomic and antigenomic RNAs1. The RSV polymerase initiates RNA synthesis by binding to the conserved 3′-terminal RNA promoters of the genome or antigenome2. However, the lack of a structure of the RSV polymerase bound to the RNA promoter has impeded the mechanistic understanding of RSV RNA synthesis. Here we report cryogenic electron microscopy structures of the RSV polymerase bound to its genomic and antigenomic viral RNA promoters, representing two of the first structures of an RNA-dependent RNA polymerase in complex with its RNA promoters in non-segmented negative-sense RNA viruses. The overall structures of the promoter-bound RSV polymerases are similar to that of the unbound (apo) polymerase. Our structures illustrate the interactions between the RSV polymerase and the RNA promoters and provide the structural basis for the initiation of RNA synthesis at positions 1 and 3 of the RSV promoters. These structures offer a deeper understanding of the pre-initiation state of the RSV polymerase and could aid in antiviral research against RSV.

Date: 2024
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DOI: 10.1038/s41586-023-06867-y

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