A novel function of the N-terminal domain of PA in assembly of influenza A virus RNA polymerase

2011 ◽  
Vol 414 (4) ◽  
pp. 719-726 ◽  
Author(s):  
Tadaki Suzuki ◽  
Akira Ainai ◽  
Noriyo Nagata ◽  
Tetsutaro Sata ◽  
Hirofumi Sawa ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Influenza A Virus ◽  
Influenza A ◽  
Terminal Domain ◽  
Virus Rna

scholarly journals Artificial Hybrids of Influenza A Virus RNA Polymerase Reveal PA Subunit Modulates Its Thermal Sensitivity

PLoS ONE ◽  
2010 ◽  
Vol 5 (12) ◽  
pp. e15140 ◽  
Author(s):  
Takahito Kashiwagi ◽  
Koyu Hara ◽  
Yoko Nakazono ◽  
Nobuyuki Hamada ◽  
Hiroshi Watanabe
Keyword(s):  
Rna Polymerase ◽  
Influenza A Virus ◽  
Influenza A ◽  
Thermal Sensitivity ◽  
Virus Rna

scholarly journals Recruitment of RED-SMU1 Complex by Influenza A Virus RNA Polymerase to Control Viral mRNA Splicing

2014 ◽  
Vol 10 (6) ◽  
pp. e1004164 ◽  
Author(s):  
Guillaume Fournier ◽  
Chiayn Chiang ◽  
Sandie Munier ◽  
Andru Tomoiu ◽  
Caroline Demeret ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Influenza A Virus ◽  
Influenza A ◽  
Mrna Splicing ◽  
Viral Mrna ◽  
Virus Rna

scholarly journals Influenza A Virus RNA Polymerase Subunit PB2 Is the Endonuclease Which Cleaves Host Cell mRNA and Functions Only as the Trimeric Enzyme

Virology ◽  
1995 ◽  
Vol 208 (1) ◽  
pp. 38-47 ◽  
Author(s):  
Licheng Shi ◽  
Donald F. Summers ◽  
Qinghai Peng ◽  
Jose M. Galarza
Keyword(s):  
Rna Polymerase ◽  
Host Cell ◽  
Influenza A Virus ◽  
Influenza A ◽  
Virus Rna

scholarly journals Role of the PB2 627 Domain in Influenza A Virus Polymerase Function

2017 ◽  
Vol 91 (7) ◽  
Author(s):  
Benjamin E. Nilsson ◽  
Aartjan J. W. te Velthuis ◽  
Ervin Fodor
Keyword(s):  
Influenza Virus ◽  
Rna Polymerase ◽  
Influenza A Virus ◽  
Influenza A ◽  
Influenza A Viruses ◽  
Viral Polymerase ◽  
Virus Rna ◽  
Rna Genome ◽  
Transcription And Replication

ABSTRACT The RNA genome of influenza A viruses is transcribed and replicated by the viral RNA-dependent RNA polymerase, composed of the subunits PA, PB1, and PB2. High-resolution structural data revealed that the polymerase assembles into a central polymerase core and several auxiliary highly flexible, protruding domains. The auxiliary PB2 cap-binding and the PA endonuclease domains are both involved in cap snatching, but the role of the auxiliary PB2 627 domain, implicated in host range restriction of influenza A viruses, is still poorly understood. In this study, we used structure-guided truncations of the PB2 subunit to show that a PB2 subunit lacking the 627 domain accumulates in the cell nucleus and assembles into a heterotrimeric polymerase with PB1 and PA. Furthermore, we showed that a recombinant viral polymerase lacking the PB2 627 domain is able to carry out cap snatching, cap-dependent transcription initiation, and cap-independent ApG dinucleotide extension in vitro, indicating that the PB2 627 domain of the influenza virus RNA polymerase is not involved in core catalytic functions of the polymerase. However, in a cellular context, the 627 domain is essential for both transcription and replication. In particular, we showed that the PB2 627 domain is essential for the accumulation of the cRNA replicative intermediate in infected cells. Together, these results further our understanding of the role of the PB2 627 domain in transcription and replication of the influenza virus RNA genome. IMPORTANCE Influenza A viruses are a major global health threat, not only causing disease in both humans and birds but also placing significant strains on economies worldwide. Avian influenza A virus polymerases typically do not function efficiently in mammalian hosts and require adaptive mutations to restore polymerase activity. These adaptations include mutations in the 627 domain of the PB2 subunit of the viral polymerase, but it still remains to be established how these mutations enable host adaptation on a molecular level. In this report, we characterize the role of the 627 domain in polymerase function and offer insights into the replication mechanism of influenza A viruses.

Structure-Based Virtual Screening for Potential Inhibitors of Influenza A Virus RNA Polymerase PA Subunit

2014 ◽  
Vol 21 (1) ◽  
pp. 149-156 ◽  
Author(s):  
Haixin Ai ◽  
Fangliang Zheng ◽  
Fangbo Deng ◽  
Chunyu Zhu ◽  
Ying Gu ◽  
...  
Keyword(s):  
Virtual Screening ◽  
Rna Polymerase ◽  
Influenza A Virus ◽  
Influenza A ◽  
Virus Rna ◽  
Potential Inhibitors
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