tetano
Editor, Senior Moderator
Front Microbiol. 2017 Apr 21;8:692. doi: 10.3389/fmicb.2017.00692. eCollection 2017.
[h=1]Amino Acid Residues 68-71 Contribute to Influenza A Virus PB1-F2 Protein Stability and Functions.[/h] Cheng YY[SUP]1,[/SUP][SUP]2[/SUP], Yang SR[SUP]1[/SUP], Wang YT[SUP]1[/SUP], Lin YH[SUP]1[/SUP], Chen CJ[SUP]1[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] Influenza A virus PB1-F2, encoding a multi-functional protein, is regarded as a virulent gene. Variation in expression pattern and protein stability among PB1-F2 proteins derived from different strains may explain why PB1-F2 functions in a strain- and cell type-specific manner. Because the protein stability of PB1-F2 affects its biological functions, we looked for sequences important for this property. By comparing variants and chimeric of PB1-F2 proteins from A/Hong Kong/156/1997 (H5N1) and A/Puerto Rico/8/1934 (H1N1), we identified amino acid residues 68-71 affect its protein stability. PB1-F2 with T68, Q69, D70, and S71 has a shorter protein half-life than its I68, L69, V70, and F71 counterpart. This is likely to do with proteasome-mediated degradation. Swapping amino acids 68-71 between two proteins reversed not only the length of protein half-life and sensitivity to MG132, but also subcellular localization and interferon antagonization. Our data suggested that composition of amino acids 68-71, which regulates protein stability and therefore its functions, can be a major factor determining strain-specificity of PB1-F2.
[h=4]KEYWORDS:[/h] PB1-F2; influenza A virus; interferon antagonism; mitochondrial localization; protein stability
PMID: 28484439 PMCID: PMC5399091 DOI: 10.3389/fmicb.2017.00692
[h=1]Amino Acid Residues 68-71 Contribute to Influenza A Virus PB1-F2 Protein Stability and Functions.[/h] Cheng YY[SUP]1,[/SUP][SUP]2[/SUP], Yang SR[SUP]1[/SUP], Wang YT[SUP]1[/SUP], Lin YH[SUP]1[/SUP], Chen CJ[SUP]1[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] Influenza A virus PB1-F2, encoding a multi-functional protein, is regarded as a virulent gene. Variation in expression pattern and protein stability among PB1-F2 proteins derived from different strains may explain why PB1-F2 functions in a strain- and cell type-specific manner. Because the protein stability of PB1-F2 affects its biological functions, we looked for sequences important for this property. By comparing variants and chimeric of PB1-F2 proteins from A/Hong Kong/156/1997 (H5N1) and A/Puerto Rico/8/1934 (H1N1), we identified amino acid residues 68-71 affect its protein stability. PB1-F2 with T68, Q69, D70, and S71 has a shorter protein half-life than its I68, L69, V70, and F71 counterpart. This is likely to do with proteasome-mediated degradation. Swapping amino acids 68-71 between two proteins reversed not only the length of protein half-life and sensitivity to MG132, but also subcellular localization and interferon antagonization. Our data suggested that composition of amino acids 68-71, which regulates protein stability and therefore its functions, can be a major factor determining strain-specificity of PB1-F2.
[h=4]KEYWORDS:[/h] PB1-F2; influenza A virus; interferon antagonism; mitochondrial localization; protein stability
PMID: 28484439 PMCID: PMC5399091 DOI: 10.3389/fmicb.2017.00692