Chikungunya virus (CHIKV) is a highly pathogenic alphavirus representative, and its nonstructural protein 2 (nsP2) plays critical roles in both inhibition of transcription and CPE development.
A strong polar interaction was predicted between Thr-180 (within the phosphorylation lip) of p38 and Gln-273 of nsP2, whereas, no such polar interaction was predicted for the phosphorylation lip of JNK which indicates the differential roles of p-p38 and p-JNK during CHIKV infection in the host macrophages.
Chikungunya virus (CHIKV) is a highly pathogenic alphavirus representative, and its nonstructural protein 2 (nsP2) plays critical roles in both inhibition of transcription and CPE development.
A strong polar interaction was predicted between Thr-180 (within the phosphorylation lip) of p38 and Gln-273 of nsP2, whereas, no such polar interaction was predicted for the phosphorylation lip of JNK which indicates the differential roles of p-p38 and p-JNK during CHIKV infection in the host macrophages.
In the present study, a FRET based protease assay was used to analyze the proteolytic activity of chikungunyansP2 protease (CHIKV nsP2pro) - an essential viral enzyme, with fluorogenic substrate peptide.
This demonstrates that the C-terminal domain of nuclear nsP2 specifically inhibits the IFN response by promoting the nuclear export of STAT1.<b>IMPORTANCE</b> Chikungunya virus is an emerging pathogen associated with large outbreaks on the African, Asian, European, and both American continents.
In the present study, a FRET based protease assay was used to analyze the proteolytic activity of chikungunyansP2 protease (CHIKV nsP2pro) - an essential viral enzyme, with fluorogenic substrate peptide.
This demonstrates that the C-terminal domain of nuclear nsP2 specifically inhibits the IFN response by promoting the nuclear export of STAT1.<b>IMPORTANCE</b> Chikungunya virus is an emerging pathogen associated with large outbreaks on the African, Asian, European, and both American continents.