tetano
Editor, Senior Moderator
FASEB J
. 2023 Feb;37(2):e22729.
doi: 10.1096/fj.202201239RR.
Influenza virus replication is affected by glutaredoxin1-mediated protein deglutathionylation
Paola Checconi[SUP] 1 2 [/SUP], Cristiana Coni[SUP] 1 2 [/SUP], Dolores Limongi[SUP] 1 2 [/SUP], Sara Baldelli[SUP] 1 3 [/SUP], Fabio Ciccarone[SUP] 3 4 [/SUP], Marta De Angelis[SUP] 5 [/SUP], Manuela Mengozzi[SUP] 6 [/SUP], Pietro Ghezzi[SUP] 7 [/SUP], Maria Rosa Ciriolo[SUP] 3 4 [/SUP], Lucia Nencioni[SUP] 5 [/SUP], Anna Teresa Palamara[SUP] 5 8 [/SUP]
Affiliations
Abstract
Several redox modifications have been described during viral infection, including influenza virus infection, but little is known about glutathionylation and this respiratory virus. Glutathionylation is a reversible, post-translational modification, in which protein cysteine forms transient disulfides with glutathione (GSH), catalyzed by cellular oxidoreductases and in particular by glutaredoxin (Grx). We show here that (i) influenza virus infection induces protein glutathionylation, including that of viral proteins such as hemagglutinin (HA); (ii) Grx1-mediated deglutathionylation is important for the viral life cycle, as its inhibition, either with an inhibitor of its enzymatic activity or by siRNA, decreases viral replication. Overall these data contribute to the characterization of the complex picture of redox regulation of the influenza virus replication cycle and could help to identify new targets to control respiratory viral infection.
Keywords: deglutathionylation; glutaredoxin1; glutathione; glutathionylation; influenza virus; redox-regulation.
. 2023 Feb;37(2):e22729.
doi: 10.1096/fj.202201239RR.
Influenza virus replication is affected by glutaredoxin1-mediated protein deglutathionylation
Paola Checconi[SUP] 1 2 [/SUP], Cristiana Coni[SUP] 1 2 [/SUP], Dolores Limongi[SUP] 1 2 [/SUP], Sara Baldelli[SUP] 1 3 [/SUP], Fabio Ciccarone[SUP] 3 4 [/SUP], Marta De Angelis[SUP] 5 [/SUP], Manuela Mengozzi[SUP] 6 [/SUP], Pietro Ghezzi[SUP] 7 [/SUP], Maria Rosa Ciriolo[SUP] 3 4 [/SUP], Lucia Nencioni[SUP] 5 [/SUP], Anna Teresa Palamara[SUP] 5 8 [/SUP]
Affiliations
- PMID: 36583688
- DOI: 10.1096/fj.202201239RR
Abstract
Several redox modifications have been described during viral infection, including influenza virus infection, but little is known about glutathionylation and this respiratory virus. Glutathionylation is a reversible, post-translational modification, in which protein cysteine forms transient disulfides with glutathione (GSH), catalyzed by cellular oxidoreductases and in particular by glutaredoxin (Grx). We show here that (i) influenza virus infection induces protein glutathionylation, including that of viral proteins such as hemagglutinin (HA); (ii) Grx1-mediated deglutathionylation is important for the viral life cycle, as its inhibition, either with an inhibitor of its enzymatic activity or by siRNA, decreases viral replication. Overall these data contribute to the characterization of the complex picture of redox regulation of the influenza virus replication cycle and could help to identify new targets to control respiratory viral infection.
Keywords: deglutathionylation; glutaredoxin1; glutathione; glutathionylation; influenza virus; redox-regulation.