scholarly journals Mutational analysis of the conserved motifs of influenza A virus polymerase basic protein 1.

1994 ◽  
Vol 68 (3) ◽  
pp. 1819-1826 ◽  
Author(s):  
S K Biswas ◽  
D P Nayak
Keyword(s):  
Influenza A Virus ◽  
Influenza A ◽  
Basic Protein ◽  
Mutational Analysis ◽  
Conserved Motifs

scholarly journals Influenza A Virus: Phylogeny of Neuraminidase Primers and Amplification of Polymerase Basic Protein 2 and Neuraminidase Genes

2009 ◽  
Vol 3 (1) ◽  
pp. 1-11
Author(s):  
MARIA OMEGA ◽  
RICHARD LAI ◽  
HANS HEINE ◽  
ROSS BARNARD
Keyword(s):  
Influenza A Virus ◽  
Influenza A ◽  
Basic Protein

scholarly journals Key amino acid residues of neuraminidase involved in influenza A virus entry

2019 ◽  
Vol 77 (6) ◽  
Author(s):  
Fangzhao Chen ◽  
Teng Liu ◽  
Jiagui Xu ◽  
Yingna Huang ◽  
Shuwen Liu ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Amino Acid ◽  
Influenza A Virus ◽  
Viral Entry ◽  
Influenza A ◽  
Mutational Analysis ◽  
Critical Role ◽  
Target Cells ◽  
Amino Acid Residues ◽  
Influenza Virus Neuraminidase

ABSTRACT Generally, influenza virus neuraminidase (NA) plays a critical role in the release stage of influenza virus. Recently, it has been found that NA may promote influenza virus to access the target cells. However, the mechanism remain unclear. Here, we reported that peramivir indeed possessed anti-influenza A virus (IAV) activity in the stage of viral entry. Importantly, we verified the critical residues of influenza NA involved in the viral entry. As a result, peramivir as an efficient NA inhibitor could suppress the initiation of IAV infection. Furthermore, mutational analysis showed NA might be associated with viral entry via amino acids residues R118, E119, D151, R152, W178, I222, E227, E276, R292 and R371. Our results demonstrated NA must contain the key amino acid residues can involve in IAV entry.

scholarly journals Mutational analysis of the RNA-fork model of the influenza A virus vRNA promoter in vivo.

1997 ◽  
Vol 78 (2) ◽  
pp. 353-357 ◽  
Author(s):  
H J Kim ◽  
B L Seong ◽  
G G Brownlee ◽  
E Fodor
Keyword(s):  
Influenza A Virus ◽  
Influenza A ◽  
Mutational Analysis

scholarly journals Mutational Analysis of Influenza A Virus Nucleoprotein: Identification of Mutations That Affect RNA Replication

1999 ◽  
Vol 73 (2) ◽  
pp. 1186-1194 ◽  
Author(s):  
Ignacio Mena ◽  
Enrique Jambrina ◽  
Carmen Albo ◽  
Beatriz Perales ◽  
Juan Ortín ◽  
...  
Keyword(s):  
Influenza A Virus ◽  
Influenza A ◽  
Rna Binding ◽  
Mutational Analysis ◽  
Intracellular Localization ◽  
Single Amino Acid ◽  
Temperature Sensitive ◽  
Virus Mutant

ABSTRACT The influenza A virus nucleoprotein (NP) is a multifunctional polypeptide which plays a pivotal role in virus replication. To get information on the domains and specific residues involved in the different NP activities, we describe here the preparation and characterization of 20 influenza A virus mutant NPs. The mutations, mostly single-amino-acid substitutions, were introduced in a cDNA copy of the A/Victoria/3/75 NP gene and, in most cases, affected residues located in regions that were highly conserved across the NPs of influenza A, B, and C viruses. The mutant NPs were characterized (i) in vivo (cell culture) by analyzing their intracellular localization and their functionality in replication, transcription, and expression of model RNA templates; and (ii) in vitro by analyzing their RNA-binding and sedimentation properties. The results obtained allowed us to identify both a mutant protein that accumulated in the cytoplasm and mutations that altered the functionality and/or the oligomerization state of the NP polypeptide. Among the mutations that reduced the NP capability to express chloramphenicol acetyltransferase protein from a model viral RNA (vRNA) template, some displayed a temperature-sensitive phenotype. Interestingly, four mutant NPs, which showed a reduced functionality in synthesizing cRNA molecules from a vRNA template, were fully competent to reconstitute complementary ribonucleoproteins (cRNPs) capable of synthesizing vRNAs, which in turn yielded mRNA molecules. Based on the phenotype of these mutants and on previously published observations, it is proposed that these mutant NPs have a reduced capability to interact with the polymerase complex and that this NP-polymerase interaction is responsible for making vRNPs switch from mRNA to cRNA synthesis.

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