Intrinsic Disorder to Order Transitions in the Scaffold Phosphoprotein P from the Respiratory Syncytial Virus RNA Polymerase Complex

Biochemistry ◽  
2016 ◽  
Vol 55 (10) ◽  
pp. 1441-1454 ◽  
Author(s):  
María G. Noval ◽  
Sebastian A. Esperante ◽  
Ivana G. Molina ◽  
Lucía B. Chemes ◽  
Gonzalo de Prat-Gay
Keyword(s):  
Respiratory Syncytial Virus ◽  
Rna Polymerase ◽  
Intrinsic Disorder ◽  
Polymerase Complex ◽  
Virus Rna ◽  
Syncytial Virus

Biochemical Characterization of Respiratory Syncytial Virus RNA-Dependent RNA Polymerase Complex

2020 ◽  
Vol 6 (10) ◽  
pp. 2800-2811
Author(s):  
Anand Balakrishnan ◽  
Edmund Price ◽  
Catherine Luu ◽  
Jacob Shaul ◽  
Charles Wartchow ◽  
...  
Keyword(s):  
Respiratory Syncytial Virus ◽  
Rna Polymerase ◽  
Biochemical Characterization ◽  
Rna Dependent Rna Polymerase ◽  
Polymerase Complex ◽  
Virus Rna ◽  
Syncytial Virus

scholarly journals Cryo-EM structure of the respiratory syncytial virus RNA polymerase

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Dongdong Cao ◽  
Yunrong Gao ◽  
Claire Roesler ◽  
Samantha Rice ◽  
Paul D’Cunha ◽  
...  
Keyword(s):  
Respiratory Syncytial Virus ◽  
Rna Polymerase ◽  
Virus Rna ◽  
Syncytial Virus

Discovery of a potent respiratory syncytial virus RNA polymerase inhibitor

2013 ◽  
Vol 23 (24) ◽  
pp. 6789-6793 ◽  
Author(s):  
Hui Xiong ◽  
Melinda Foulk ◽  
Lisa Aschenbrenner ◽  
Jun Fan ◽  
Choi-Lai Tiong-Yip ◽  
...  
Keyword(s):  
Respiratory Syncytial Virus ◽  
Rna Polymerase ◽  
Virus Rna ◽  
Polymerase Inhibitor ◽  
Syncytial Virus

scholarly journals Molecular Basis for the Selective Inhibition of Respiratory Syncytial Virus RNA Polymerase by 2'-Fluoro-4'-Chloromethyl-Cytidine Triphosphate

2015 ◽  
Vol 11 (6) ◽  
pp. e1004995 ◽  
Author(s):  
Jerome Deval ◽  
Jin Hong ◽  
Guangyi Wang ◽  
Josh Taylor ◽  
Lucas K. Smith ◽  
...  
Keyword(s):  
Respiratory Syncytial Virus ◽  
Rna Polymerase ◽  
Molecular Basis ◽  
Selective Inhibition ◽  
Virus Rna ◽  
Syncytial Virus

scholarly journals Optimization of Potent and Selective Quinazolinediones: Inhibitors of Respiratory Syncytial Virus That Block RNA-Dependent RNA-Polymerase Complex Activity

2014 ◽  
Vol 57 (24) ◽  
pp. 10314-10328 ◽  
Author(s):  
Daljit S. Matharu ◽  
Daniel P. Flaherty ◽  
Denise S. Simpson ◽  
Chad E. Schroeder ◽  
Donghoon Chung ◽  
...  
Keyword(s):  
Respiratory Syncytial Virus ◽  
Rna Polymerase ◽  
Complex Activity ◽  
Rna Dependent Rna Polymerase ◽  
Polymerase Complex ◽  
Syncytial Virus

An Amino-Proximal Domain of the L Protein Binds to the P Protein in the Measles Virus RNA Polymerase Complex

Virology ◽  
1994 ◽  
Vol 205 (2) ◽  
pp. 540-545 ◽  
Author(s):  
Sandra M. Horikami ◽  
Sherin Smallwood ◽  
Bettina Bankamp ◽  
Sue A. Moyer
Keyword(s):  
Rna Polymerase ◽  
Measles Virus ◽  
Polymerase Complex ◽  
L Protein ◽  
P Protein ◽  
Virus Rna

scholarly journals Involvement of Hsp90 in Assembly and Nuclear Import of Influenza Virus RNA Polymerase Subunits

2006 ◽  
Vol 81 (3) ◽  
pp. 1339-1349 ◽  
Author(s):  
Tadasuke Naito ◽  
Fumitaka Momose ◽  
Atsushi Kawaguchi ◽  
Kyosuke Nagata
Keyword(s):  
Influenza Virus ◽  
Rna Polymerase ◽  
Nuclear Transport ◽  
Intracellular Localization ◽  
Viral Rna ◽  
Polymerase Complex ◽  
Virus Rna ◽  
Binary Complexes ◽  
Infected Cells ◽  
Rna Polymerase Subunits

ABSTRACT Transcription and replication of the influenza virus RNA genome occur in the nuclei of infected cells through the viral RNA-dependent RNA polymerase consisting of PB1, PB2, and PA. We previously identified a host factor designated RAF-1 (RNA polymerase activating factor 1) that stimulates viral RNA synthesis. RAF-1 is found to be identical to Hsp90. Here, we examined the intracellular localization of Hsp90 and viral RNA polymerase subunits and their molecular interaction. Hsp90 was found to interact with PB2 and PB1, and it was relocalized to the nucleus upon viral infection. We found that the nuclear transport of Hsp90 occurs in cells expressing PB2 alone. The nuclear transport of Hsp90 was in parallel with that of the viral RNA polymerase binary complexes, either PB1 and PB2 or PB1 and PA, as well as with that of PB2 alone. Hsp90 also interacted with the binary RNA polymerase complex PB1-PB2, and it was dissociated from the PB1-PB2 complex upon its association with PA. Furthermore, Hsp90 could form a stable PB1-PB2-Hsp90 complex prior to the formation of a ternary polymerase complex by the assembly of PA in the infected cells. These results suggest that Hsp90 is involved in the assembly and nuclear transport of viral RNA polymerase subunits, possibly as a molecular chaperone for the polymerase subunits prior to the formation of a mature ternary polymerase complex.

scholarly journals Generation of Bovine Respiratory Syncytial Virus (BRSV) from cDNA: BRSV NS2 Is Not Essential for Virus Replication in Tissue Culture, and the Human RSV Leader Region Acts as a Functional BRSV Genome Promoter

1999 ◽  
Vol 73 (1) ◽  
pp. 251-259 ◽  
Author(s):  
Ursula J. Buchholz ◽  
Stefan Finke ◽  
Karl-Klaus Conzelmann
Keyword(s):  
Cell Culture ◽  
Respiratory Syncytial Virus ◽  
Rna Polymerase ◽  
Virus Replication ◽  
Nonstructural Protein ◽  
Bovine Respiratory Syncytial Virus ◽  
T7 Rna Polymerase ◽  
Leader Region ◽  
Successful Recovery ◽  
Syncytial Virus

ABSTRACT In order to generate recombinant bovine respiratory syncytial virus (BRSV), the genome of BRSV strain A51908, variant ATue51908, was cloned as cDNA. We provide here the sequence of the BRSV genome ends and of the entire L gene. This completes the sequence of the BRSV genome, which comprises a total of 15,140 nucleotides. To establish a vaccinia virus-free recovery system, a BHK-derived cell line stably expressing T7 RNA polymerase was generated (BSR T7/5). Recombinant BRSV was reproducibly recovered from cDNA constructs after T7 RNA polymerase-driven expression of antigenome sense RNA and of BRSV N, P, M2, and L proteins from transfected plasmids. Chimeric viruses in which the BRSV leader region was replaced by the human respiratory syncytial virus (HRSV) leader region replicated in cell culture as efficiently as their nonchimeric counterparts, demonstrating that allcis-acting sequences of the HRSV promoter are faithfully recognized by the BRSV polymerase complex. In addition, we report the successful recovery of a BRSV mutant lacking the complete NS2 gene, which encodes a nonstructural protein of unknown function. The NS2-deficient BRSV replicated autonomously and could be passaged, demonstrating that NS2 is not essential for virus replication in cell culture. However, growth of the mutant was considerably slower than and final infectious titers were reduced by a factor of at least 10 compared to wild-type BRSV, indicating that NS2 provides a supporting factor required for full replication capacity.

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