tetano
Editor, Senior Moderator
Mol Biol (Mosk). 2017 Mar-Apr;51(2):378-383. doi: 10.7868/S0026898417010141.
[h=1][Impact of mutations in nucleoprotein on replication of influenza virus A/Hong Kong/1/68/162/35 reassortants at different temperatures].[/h] [Article in Russian]
Pulkina AA[SUP]1,[/SUP][SUP]2[/SUP], Sergeeva MV[SUP]1,[/SUP][SUP]3[/SUP], Petrov SV[SUP]1[/SUP], Fadeev AV[SUP]1[/SUP], Komissarov AB[SUP]1[/SUP], Romanovskaya-Romanko EA[SUP]1[/SUP], Potapchuk MV[SUP]1[/SUP], Tsybalova LM[SUP]1[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] The nucleoprotein (NP) of influenza virus is a multifunctional RNA binding protein. The role of NP in the adaptation of influenza viruses to a host has been experimentally proved. Ambiguous data are available on the role of nucleoprotein in the attenuation of influenza A viruses, which is characterized by ability to replicate at low temperature (26?C) and inability to replicate at high temperature (39?C). Influenza virus donor strain A/Hong Kong/1/68/162/35 (H3N2), adapted to growth at low temperature, differs from the wild type virus by 14 amino acid mutations in the internal and non-structural proteins. Two mutations occurred in the NP: Gly102Arg and Glu292Gly. We have obtained viruses with point reverse-mutations in these positions and compared their replication at different temperatures by measuring infectious activity in chicken embryos. It has been shown that reverse mutation Gly292Glu in the NP reduced virus ability to replicate at low temperature, the introduction of the second reverse mutation Arg102Gly completely abolished virus cold adaptation.
[h=4]KEYWORDS:[/h] cold adapted phenotype; influenza virus nucleoprotein; reassortant; reverse-mutation; temperature sensitive phenotype
PMID: 28537245 DOI: 10.7868/S0026898417010141
[h=1][Impact of mutations in nucleoprotein on replication of influenza virus A/Hong Kong/1/68/162/35 reassortants at different temperatures].[/h] [Article in Russian]
Pulkina AA[SUP]1,[/SUP][SUP]2[/SUP], Sergeeva MV[SUP]1,[/SUP][SUP]3[/SUP], Petrov SV[SUP]1[/SUP], Fadeev AV[SUP]1[/SUP], Komissarov AB[SUP]1[/SUP], Romanovskaya-Romanko EA[SUP]1[/SUP], Potapchuk MV[SUP]1[/SUP], Tsybalova LM[SUP]1[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] The nucleoprotein (NP) of influenza virus is a multifunctional RNA binding protein. The role of NP in the adaptation of influenza viruses to a host has been experimentally proved. Ambiguous data are available on the role of nucleoprotein in the attenuation of influenza A viruses, which is characterized by ability to replicate at low temperature (26?C) and inability to replicate at high temperature (39?C). Influenza virus donor strain A/Hong Kong/1/68/162/35 (H3N2), adapted to growth at low temperature, differs from the wild type virus by 14 amino acid mutations in the internal and non-structural proteins. Two mutations occurred in the NP: Gly102Arg and Glu292Gly. We have obtained viruses with point reverse-mutations in these positions and compared their replication at different temperatures by measuring infectious activity in chicken embryos. It has been shown that reverse mutation Gly292Glu in the NP reduced virus ability to replicate at low temperature, the introduction of the second reverse mutation Arg102Gly completely abolished virus cold adaptation.
[h=4]KEYWORDS:[/h] cold adapted phenotype; influenza virus nucleoprotein; reassortant; reverse-mutation; temperature sensitive phenotype
PMID: 28537245 DOI: 10.7868/S0026898417010141