Glutathionylation of chikungunya nsP2 protein affects protease activity

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• 作者：Chonticha Saisawang^a ; Atichat Kuadkitkan^a ; Duncan R. Smith^a ; ^c ; Sukathida Ubol^b ; ^c ; Albert J. Ketterman^a ; ^{albertketterman@yahoo.com}
• 关键词：CHIKV ; Chikungunya virus ; SINV ; Sindbis virus ; SFV ; Semliki Forest virus ; VEEV ; Venezuelan equine encephalitis virus ; nsP2 ; Nonstructural protein 2 ; MBP ; Maltose-binding protein ; AGA ; Cleavage sites nsP1/nsP2 ; AGC ; nsP2/nsP3 ; AGG ; nsP3/nsP4 ; (hpi) ; Hours post-transfection
• 刊名：Biochimica et Biophysica Acta (BBA) - General Subjects
• 出版年：2017
• 出版时间：February 2017
• 年：2017
• 卷：1861
• 期：2
• 页码：106-111
• 全文大小：678 K
• 卷排序：1861

文摘

Virus infection induces oxidative stress which triggers glutathionylation events. The multifunctional chikungunya nsP2 is glutathionylated in virus-infected cells. Glutathionylation impacts upon the protease activity of nsP2. We identify 6 cysteine residues that are glutathionylated. None of the residues are in the active site suggesting conformational changes.