Strong Binding and Off–On Signaling Functions of Deep‐Red Fluorescent TO‐PRO‐3 for Influenza A Virus RNA Promoter Region

ChemBioChem ◽  
2019 ◽  
Vol 20 (21) ◽  
pp. 2752-2756 ◽  
Author(s):  
Yusuke Sato ◽  
Yuri Aiba ◽  
Sayaka Yajima ◽  
Takaaki Tanabe ◽  
Kei Higuchi ◽  
...  
Keyword(s):  
Influenza A Virus ◽  
Promoter Region ◽  
Influenza A ◽  
Strong Binding ◽  
Virus Rna ◽  
Rna Promoter

scholarly journals Cover Feature: Strong Binding and Off–On Signaling Functions of Deep‐Red Fluorescent TO‐PRO‐3 for Influenza A Virus RNA Promoter Region (ChemBioChem 21/2019)

ChemBioChem ◽  
2019 ◽  
Vol 20 (21) ◽  
pp. 2684-2684
Author(s):  
Yusuke Sato ◽  
Yuri Aiba ◽  
Sayaka Yajima ◽  
Takaaki Tanabe ◽  
Kei Higuchi ◽  
...  
Keyword(s):  
Influenza A Virus ◽  
Promoter Region ◽  
Influenza A ◽  
Strong Binding ◽  
Virus Rna ◽  
Rna Promoter

scholarly journals Biophysical Analysis of Influenza A Virus RNA Promoter at Physiological Temperatures

2011 ◽  
Vol 286 (26) ◽  
pp. 22965-22970 ◽  
Author(s):  
Erin Noble ◽  
David H. Mathews ◽  
Jonathan L. Chen ◽  
Douglas H. Turner ◽  
Toru Takimoto ◽  
...  
Keyword(s):  
Influenza A Virus ◽  
Influenza A ◽  
Virus Rna ◽  
Biophysical Analysis ◽  
Rna Promoter

scholarly journals A novel small-molecule binds to the influenza A virus RNA promoter and inhibits viral replication

2014 ◽  
Vol 50 (3) ◽  
pp. 368-370 ◽  
Author(s):  
Mi-Kyung Lee ◽  
Angel Bottini ◽  
Meehyein Kim ◽  
Michael F. Bardaro ◽  
Ziming Zhang ◽  
...  
Keyword(s):  
Viral Replication ◽  
Influenza A Virus ◽  
Small Molecule ◽  
Influenza A ◽  
Virus Rna ◽  
Rna Promoter

scholarly journals Hairpin Loop Structure in the 3′ Arm of the Influenza A Virus Virion RNA Promoter Is Required for Endonuclease Activity

2001 ◽  
Vol 75 (15) ◽  
pp. 7042-7049 ◽  
Author(s):  
Michael B. Leahy ◽  
Helen C. Dobbyn ◽  
George G. Brownlee
Keyword(s):  
Influenza Virus ◽  
Influenza A Virus ◽  
Influenza A ◽  
Point Mutations ◽  
Nucleotide Position ◽  
Loop Structure ◽  
Endonuclease Activity ◽  
Hairpin Loop ◽  
Virus Rna ◽  
Rna Promoter

ABSTRACT Previous studies have shown that the 5′ arm of the influenza A virus virion RNA promoter requires a hairpin loop structure for efficient endonuclease activity of influenza virus RNA polymerase, an activity that is required for the cap-snatching activity of primers from host pre-mRNA. Here we examine whether a hairpin loop is also required in the 3′ arm of the viral RNA promoter. We study point mutations at each nucleotide position (1 to 12) within the 3′ arm of the promoter as well as complementary “rescue” mutations which restored base pairing in the stem of a potential hairpin loop. Our results suggest that endonuclease activity is absolutely dependent on the presence of a 3′ hairpin loop structure. This is the first direct evidence for RNA secondary structure within the 3′ arm being required for a specific stage, i.e., endonuclease cleavage, in the influenza virus replicative cycle.

scholarly journals The RNA Polymerase of Influenza A Virus Is Stabilized by Interaction with Its Viral RNA Promoter

2002 ◽  
Vol 76 (14) ◽  
pp. 7103-7113 ◽  
Author(s):  
George G. Brownlee ◽  
Jane L. Sharps
Keyword(s):  
Influenza Virus ◽  
Rna Polymerase ◽  
Influenza A Virus ◽  
Influenza A ◽  
Human Kidney ◽  
Host Cells ◽  
Heat Inactivation ◽  
Virus Rna ◽  
Polymerase Binding ◽  
Rna Promoter

ABSTRACT The RNA polymerase of the influenza virus is responsible for the transcription and replication of the segmented RNA viral genome during infection of host cells. Polymerase function is known to be strictly dependent on interaction with its RNA promoter, but no attempts to investigate whether the virion RNA (vRNA) promoter stabilizes the polymerase have been reported previously. Here we tested whether the vRNA promoter protects the polymerase against heat inactivation. We prepared partially purified recombinant influenza A virus RNA polymerase, in the absence of influenza virus vRNA promoter sequences, by transient transfection of expression plasmids into human kidney 293T cells. The polymerase was found to be heat labile at 40°C in the absence of added vRNA. However, it was protected from heat inactivation if both the 5′ and 3′ strands of the vRNA promoter were present. By using the ability of vRNA to protect the enzyme against heat inactivation, we established a novel assay, in conjunction with a mutagenic approach, that was used to test the secondary structure requirement of the vRNA promoter for polymerase binding. Binding required a panhandle structure and the presence of local hairpin loop structures in both the 5′ and 3′ ends of vRNA, as suggested by the corkscrew model. The interaction of the vRNA promoter with the influenza virus RNA polymerase heterotrimeric complex is likely to favor a particular closed conformation of the complex, thereby ensuring the stability of the RNA polymerase within both the infected cell and the isolated virus.

Single-Molecule-Based Detection of Conserved Influenza A Virus RNA Promoter Using a Protein Nanopore

ACS Sensors ◽  
2019 ◽  
Vol 4 (11) ◽  
pp. 2849-2853 ◽  
Author(s):  
Sohee Oh ◽  
Mi-Kyung Lee ◽  
Seung-Wook Chi
Keyword(s):  
Influenza A Virus ◽  
Single Molecule ◽  
Influenza A ◽  
Virus Rna ◽  
Rna Promoter

scholarly journals Targeting Influenza A Virus RNA Promoter

2015 ◽  
Vol 86 (4) ◽  
pp. 663-673 ◽  
Author(s):  
Angel Bottini ◽  
Surya K. De ◽  
Bainan Wu ◽  
Changyan Tang ◽  
Gabriele Varani ◽  
...  
Keyword(s):  
Influenza A Virus ◽  
Influenza A ◽  
Virus Rna ◽  
Rna Promoter

scholarly journals Dual Roles of the Hemagglutinin Segment-Specific Noncoding Nucleotides in the Extended Duplex Region of the Influenza A Virus RNA Promoter

2016 ◽  
Vol 91 (1) ◽  
Author(s):  
Jingfeng Wang ◽  
Jinghua Li ◽  
Lili Zhao ◽  
Mengmeng Cao ◽  
Tao Deng
Keyword(s):  
Virus Infection ◽  
Influenza A Virus ◽  
Virus Replication ◽  
Influenza A ◽  
Critical Role ◽  
Virus Genome ◽  
Viral Rna ◽  
Genome Packaging ◽  
Virus Rna ◽  
Rna Promoter

ABSTRACT We recently reported that the segment-specific noncoding regions (NCRs) of the hemagglutinin (HA) and neuraminidase (NA) segments are subtype specific, varying significantly in sequence and length at both the 3′ and 5′ ends. Interestingly, we found that nucleotides CC at positions 13 and 14 at the 3′ end and GUG at positions 14 to 16 at the 5′ end (termed 14′ and 16′ to distinguish them from 3′ positions) are absolutely conserved among all HA subtype-specific NCRs. These HA segment-specific NCR nucleotides are located in the extended duplex region of the viral RNA promoter. In order to understand the significance of these highly conserved HA segment-specific NCR nucleotides in the virus life cycle, we performed extensive mutagenesis on the HA segment-specific NCR nucleotides and studied their functional significance in regulating influenza A virus replication in the context of the HA segment with both RNP reconstitution and virus infection systems. We found that the base pairing of the 3′-end 13 position with the 5′-end 14′ position (3′13-5′14′) position is critical for RNA promoter activity while the identity of the base pair is critical in determining HA segment packaging. Moreover, the identity of the residue at the 3′-end 14 position is functionally more important in regulating virus genome packaging than in regulating viral RNA synthesis. Taken together, these results demonstrated that the HA segment-specific NCR nucleotides in the extended duplex region of the promoter not only form part of the promoter but also play a key role in controlling virus selective genome packaging. IMPORTANCE The segment-specific complementary nucleotides (13 to 15 in the 3′ end and 14′ to 16′ in the 5′ end) in the extended duplex region of the influenza virus RNA promoter vary significantly among different segments and have rarely been studied. Here, we performed mutagenesis analysis of the highly conserved HA segment-specific nucleotides in the extended duplex region and examined their effects on virus replication in the context of the influenza A/WSN/33 (WSN) virus infection. We found that these HA segment-specific nucleotides not only act as a part of the RNA promoter but also play a critical role in HA segment packaging. Therefore, we showed experimentally, for the first time, the requirement of the nucleotides in the extended duplex region for the RNA promoter and also identified specific noncoding residues in regulating HA segment packaging. This work has implications for the development of attenuated vaccine strains and for elucidation the mechanisms of the virus genome packaging.

Aminoglycoside antibiotics bind to the influenza A virus RNA promoter

2012 ◽  
Vol 8 (11) ◽  
pp. 2857 ◽  
Author(s):  
Henna Kim ◽  
Mi-Kyung Lee ◽  
Junsang Ko ◽  
Chin-Ju Park ◽  
Meehyein Kim ◽  
...  
Keyword(s):  
Influenza A Virus ◽  
Influenza A ◽  
Aminoglycoside Antibiotics ◽  
Virus Rna ◽  
Rna Promoter

scholarly journals Correction: A novel small-molecule binds to the influenza A virus RNA promoter and inhibits viral replication

2014 ◽  
Vol 50 (83) ◽  
pp. 12578-12578 ◽  
Author(s):  
Mi-Kyung Lee ◽  
Angel Bottini ◽  
Meehyein Kim ◽  
Michael F. Bardaro ◽  
Ziming Zhang ◽  
...  
Keyword(s):  
Viral Replication ◽  
Influenza A Virus ◽  
Small Molecule ◽  
Influenza A ◽  
Virus Rna ◽  
Rna Promoter
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