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Role of Glutathionylation in Infection and Inflammation

IRCCS San Raffaele Pisana, Department of Human Sciences and Promotion of the Quality of Life, San Raffaele Roma Open University, 00166 Rome, Italy
Department of Biology, University of Rome Tor Vergata, 00133 Rome, Italy
Department of Public Health and Infectious Diseases, laboratory affiliated to Istituto Pasteur Italia-Fondazione Cenci Bolognetti, Sapienza University of Rome, 00185 Rome, Italy
Author to whom correspondence should be addressed.
These authors contributed equally to the work.
Nutrients 2019, 11(8), 1952;
Received: 26 June 2019 / Revised: 9 August 2019 / Accepted: 16 August 2019 / Published: 20 August 2019
(This article belongs to the Special Issue Glutathione Metabolism)
Glutathionylation, that is, the formation of mixed disulfides between protein cysteines and glutathione (GSH) cysteines, is a reversible post-translational modification catalyzed by different cellular oxidoreductases, by which the redox state of the cell modulates protein function. So far, most studies on the identification of glutathionylated proteins have focused on cellular proteins, including proteins involved in host response to infection, but there is a growing number of reports showing that microbial proteins also undergo glutathionylation, with modification of their characteristics and functions. In the present review, we highlight the signaling role of GSH through glutathionylation, particularly focusing on microbial (viral and bacterial) glutathionylated proteins (GSSPs) and host GSSPs involved in the immune/inflammatory response to infection; moreover, we discuss the biological role of the process in microbial infections and related host responses. View Full-Text
Keywords: glutathione; glutathionylation; redox signaling; infection; inflammation glutathione; glutathionylation; redox signaling; infection; inflammation
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Checconi, P.; Limongi, D.; Baldelli, S.; Ciriolo, M.R.; Nencioni, L.; Palamara, A.T. Role of Glutathionylation in Infection and Inflammation. Nutrients 2019, 11, 1952.

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