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18. Molecular Determinants of Pathogenicity in the Polymerase Complex

Author

Gabriel, Gülsah, Fodor, Ervin, Compans, Richard W, Series editor, Cooper, Max D., Series editor, Gleba, Yuri Y., Series editor, Honjo, Tasuku, Series editor, Oldstone, Michael B. A., Series editor, Vogt, Peter K., Series editor, Malissen, Bernard, Series editor, Aktories, Klaus, Series editor, Kawaoka, Yoshihiro, Series editor, Rappuoli, Rino, Series editor, Galan, Jorge E., Series editor, Ahmed, Rafi, Series editor, and Compans, Richard W., editor

Published
2014
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23. Crystal structure of the RNA-dependent RNA polymerase from influenza C virus

Author

Hengrung, Narin, Omari, Kamel El, Martin, Itziar Serna, Vreede, Frank T., Cusack, Stephen, Rambo, Robert P., Vonrhein, Clemens, Bricogne, Gerard, Stuart, David I., Grimes, Jonathan M., and Fodor, Ervin

Subjects
RNA polymerases -- Structure, Crystals -- Structure, Influenza viruses -- Physiological aspects -- Genetic aspects, Microbiological research, Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

Negative-sense RNA viruses, such as influenza, encode large, multidomain RNA-dependent RNA polymerases that can both transcribe and replicate the viral RNA genome (1). In influenza virus, the polymerase (FluPol) is [...]

Published
2015

26. Characterization of the SARS-CoV-2 ExoN (nsp14ExoN–nsp10) complex: implications for its role in viral genome stability and inhibitor identification

Author

Baddock, Hannah T, primary, Brolih, Sanja, additional, Yosaatmadja, Yuliana, additional, Ratnaweera, Malitha, additional, Bielinski, Marcin, additional, Swift, Lonnie P, additional, Cruz-Migoni, Abimael, additional, Fan, Haitian, additional, Keown, Jeremy R, additional, Walker, Alexander P, additional, Morris, Garrett M, additional, Grimes, Jonathan M, additional, Fodor, Ervin, additional, Schofield, Christopher J, additional, Gileadi, Opher, additional, and McHugh, Peter J, additional

Published
2022
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33. Crystal structure of an avian influenza polymerase [PA.sub.N] reveals an endonuclease active site

Author

Yuan, Puwei, Bartlam, Mark, Lou, Zhiyong, Chen, Shoudeng, Zhou, Jie, He, Xiaojing, Lv, Zongyang, Ge, Ruowen, Li, Xuemei, Deng, Tao, Fodor, Ervin, Rao, Zihe, and Liu, Yingfang

Subjects
RNA polymerases -- Structure -- Research -- Physiological aspects, Binding sites (Biochemistry) -- Research -- Physiological aspects, Avian influenza -- Research -- Physiological aspects, Environmental issues, Science and technology, Zoology and wildlife conservation, Structure, Physiological aspects, Research
Abstract

The heterotrimeric influenza virus polymerase, containing the PA, PB1 and PB2 proteins, catalyses viral RNA replication and transcription in the nucleus of infected cells. PBI holds the polymerase active site (1) and reportedly harbours endonuclease activity (2), whereas PB2 is responsible for cap binding (2-4). The PA amino terminus is understood to be the major functional part of the PA protein and has been implicated in several roles, including endonuclease (5) and protease activities (6) as well as viral RNA/complementary RNA promoter binding (7). Here we report the 2.2 angstrom (Å) crystal structure of the N-terminal 197 residues of PA, termed [PA.sub.N], from an avian influenza H5N1 virus. The [PA.sub.N] structure has an α/β architecture and reveals a bound magnesium ion coordinated by a motif similar to the (P)[DX.sub.N](D/E)XK motif characteristic of many endonucleases. Structural comparisons and mutagenesis analysis of the motif identified in PAN provide further evidence that [PA.sub.N] holds an endonuclease active site. Furthermore, functional analysis with in vivo ribonucleoprotein reconstitution and direct in vitro endonuclease assays strongly suggest that PAN holds the endonuclease active site and has critical roles in endonuclease activity of the influenza virus polymerase, rather than PB1. The high conservation of this endonuclease active site among influenza strains indicates that [PA.sub.N] is an important target for the design of new anti-influenza therapeutics., Highly pathogenic avian influenza A virus strains with H5N1 subtype are entrenched in poultry worldwide and pose a growing threat to human health. Of the 387 reported human cases of [...]

Published
2009

40. Design, Synthesis, and Biological Evaluation of Novel Indoles Targeting the Influenza PB2 Cap Binding Region

Author

McGowan, David C., primary, Balemans, Wendy, additional, Embrechts, Werner, additional, Motte, Magali, additional, Keown, Jeremy R., additional, Buyck, Christophe, additional, Corbera, Jordi, additional, Funes, Mario, additional, Moreno, Laura, additional, Cooymans, Ludwig, additional, Tahri, Abdellah, additional, Eymard, Julien, additional, Stoops, Bart, additional, Strijbos, Rudy, additional, Van den Berg, Joke, additional, Fodor, Ervin, additional, Grimes, Jonathan M., additional, Koul, Anil, additional, Jonckers, Tim H. M., additional, Raboisson, Pierre, additional, and Guillemont, Jérôme, additional

Published
2019
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43. The surface-exposed PA51-72-loop of the influenza A virus polymerase is required for viral genome replication

Author

Nilsson-Payant, Benjamin E., Sharps, Jane, Hengrung, Narin, and Fodor, Ervin

Subjects
replication, viruses, RNA-Dependent RNA Polymerase, Virus Replication, influenza virus, Genome Replication and Regulation of Viral Gene Expression, Viral Proteins, RNA polymerase, Influenza A virus, RNA, Viral, Mutant Proteins, PA subunit, Protein Multimerization, transcription, PA51-72-loop, Protein Binding, Sequence Deletion
Abstract

Influenza A viruses are a major global health threat, not only causing significant morbidity and mortality every year but also having the potential to cause severe pandemic outbreaks like the 1918 influenza pandemic. The viral polymerase is a protein complex which is responsible for transcription and replication of the viral genome and therefore is an attractive target for antiviral drug development. For that purpose it is important to understand the mechanisms of how the virus replicates its genome and how the viral polymerase works on a molecular level. In this report, we characterize the role of the flexible surface-exposed PA51-72-loop in polymerase function and offer new insights into the replication mechanism of influenza A viruses., The heterotrimeric influenza A virus RNA-dependent RNA polymerase complex, composed of PB1, PB2, and PA subunits, is responsible for transcribing and replicating the viral RNA genome. The N-terminal endonuclease domain of the PA subunit performs endonucleolytic cleavage of capped host RNAs to generate capped RNA primers for viral transcription. A surface-exposed flexible loop (PA51-72-loop) in the PA endonuclease domain has been shown to be dispensable for endonuclease activity. Interestingly, the PA51-72-loop was found to form different intramolecular interactions depending on the conformational arrangement of the polymerase. In this study, we show that a PA subunit lacking the PA51-72-loop assembles into a heterotrimeric polymerase with PB1 and PB2. We demonstrate that in a cellular context, the PA51-72-loop is required for RNA replication but not transcription by the viral polymerase. In agreement, recombinant viral polymerase lacking the PA51-72-loop is able to carry out cap-dependent transcription but is inhibited in de novo replication initiation in vitro. Furthermore, viral RNA (vRNA) synthesis is also restricted during ApG-primed extension, indicating that the PA51-72-loop is required not only for replication initiation but also for elongation on a cRNA template. We propose that the PA51-72-loop plays a role in the stabilization of the replicase conformation of the polymerase. Together, these results further our understanding of influenza virus RNA genome replication in general and highlight a role of the PA endonuclease domain in polymerase function in particular. IMPORTANCE Influenza A viruses are a major global health threat, not only causing significant morbidity and mortality every year but also having the potential to cause severe pandemic outbreaks like the 1918 influenza pandemic. The viral polymerase is a protein complex which is responsible for transcription and replication of the viral genome and therefore is an attractive target for antiviral drug development. For that purpose it is important to understand the mechanisms of how the virus replicates its genome and how the viral polymerase works on a molecular level. In this report, we characterize the role of the flexible surface-exposed PA51-72-loop in polymerase function and offer new insights into the replication mechanism of influenza A viruses.

Published
2018

50. Mini viral RNAs act as innate immune agonists during influenza virus infection

Author

Velthuis, Aartjan J.W. te, primary, Long, Joshua C., additional, Bauer, David L.V., additional, Fan, Rebecca L.Y., additional, Yen, Hui-Ling, additional, Sharps, Jane, additional, Siegers, Jurre Y., additional, Killip, Marian J., additional, French, Hollie, additional, José Oliva-Martín, Maria, additional, Randall, Richard E., additional, Wit, Emmie de, additional, Riel, Debby van, additional, Poon, Leo L.M., additional, and Fodor, Ervin, additional

Published
2018
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