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 ◽  
...  
2014 ◽  
Vol 50 (3) ◽  
pp. 368-370 ◽  
Author(s):  
Mi-Kyung Lee ◽  
Angel Bottini ◽  
Meehyein Kim ◽  
Michael F. Bardaro ◽  
Ziming Zhang ◽  
...  

2011 ◽  
Vol 286 (26) ◽  
pp. 22965-22970 ◽  
Author(s):  
Erin Noble ◽  
David H. Mathews ◽  
Jonathan L. Chen ◽  
Douglas H. Turner ◽  
Toru Takimoto ◽  
...  

2016 ◽  
Vol 71 (9) ◽  
pp. 2489-2497 ◽  
Author(s):  
Shuofeng Yuan ◽  
Hin Chu ◽  
Ke Zhang ◽  
Jiahui Ye ◽  
Kailash Singh ◽  
...  

ChemBioChem ◽  
2019 ◽  
Vol 20 (21) ◽  
pp. 2684-2684
Author(s):  
Yusuke Sato ◽  
Yuri Aiba ◽  
Sayaka Yajima ◽  
Takaaki Tanabe ◽  
Kei Higuchi ◽  
...  

ChemBioChem ◽  
2019 ◽  
Vol 20 (21) ◽  
pp. 2752-2756 ◽  
Author(s):  
Yusuke Sato ◽  
Yuri Aiba ◽  
Sayaka Yajima ◽  
Takaaki Tanabe ◽  
Kei Higuchi ◽  
...  

2019 ◽  
Author(s):  
Haili Zhang ◽  
Zhenyu Zhang ◽  
Yujie Wang ◽  
Meiyue Wang ◽  
Xuefeng Wang ◽  
...  

ABSTRACTThe polymerase of the influenza virus is part of the key machinery necessary for viral replication. However, the avian influenza virus polymerase is restricted in mammalian cells. The cellular protein ANP32A has been recently found to interact with viral polymerase, and to both influence polymerase activity and interspecies restriction. Here we report that either ANP32A or ANP32B is indispensable for influenza A virus RNA replication. The contribution of ANP32B is equal to that of ANP32A, and together they play a fundamental role in the activity of mammalian influenza A virus polymerase, while neither human ANP32A nor ANP32B support the activity of avian viral polymerase. Interestingly, we found that avian ANP32B was naturally inactive, leaving ANP32A alone to support viral replication. Two amino acid mutations at sites 129-130 in chicken ANP32B lead to the loss of support of viral replication and weak interaction with the viral polymerase complex, and these amino acids are also crucial in the maintenance of viral polymerase activity in other ANP32 proteins. Our findings strongly support ANP32A&B as key factors for both virus replication and adaption.IMPORTANCEThe key host factors involved in the influenza A viral the polymerase activity and RNA replication remain largely unknown. Here we provide evidence that ANP32A and ANP32B from different species are powerful factors in the maintenance of viral polymerase activity. Human ANP32A and ANP32B contribute equally to support human influenza virus RNA replication. However, unlike avian ANP32A, the avian ANP32B is evolutionarily non-functional in supporting viral replication because of a 129-130 site mutation. The 129-130 site plays an important role in ANP32A/B and viral polymerase interaction, therefore determine viral replication, suggesting a novel interface as a potential target for the development of anti-influenza strategies.


2001 ◽  
Vol 75 (15) ◽  
pp. 7042-7049 ◽  
Author(s):  
Michael B. Leahy ◽  
Helen C. Dobbyn ◽  
George G. Brownlee

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.


2002 ◽  
Vol 76 (14) ◽  
pp. 7103-7113 ◽  
Author(s):  
George G. Brownlee ◽  
Jane L. Sharps

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.


ACS Sensors ◽  
2019 ◽  
Vol 4 (11) ◽  
pp. 2849-2853 ◽  
Author(s):  
Sohee Oh ◽  
Mi-Kyung Lee ◽  
Seung-Wook Chi

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

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