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Review
. 2019 Aug 20;11(8):1952.
doi: 10.3390/nu11081952.

Role of Glutathionylation in Infection and Inflammation

Paola Checconi  1 , Dolores Limongi  2 , Sara Baldelli  2 , Maria Rosa Ciriolo  2   3 , Lucia Nencioni  4 , Anna Teresa Palamara  2   4
Affiliations
Review

Role of Glutathionylation in Infection and Inflammation

Paola Checconi et al. Nutrients. .

Abstract

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.

Keywords: glutathione; glutathionylation; infection; inflammation; redox signaling.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Biochemical reactions through which glutathionylated proteins can be formed and a list of proteins that have been shown to undergo glutathionylation in viruses (a), bacteria (b), or cellular immune/inflammatory pathways (c).
Figure 2
Figure 2
Diagram summarizing the effect or biological role, known or proposed, of glutathionylation on proteins described in this review, including the relevant references.
See this image and copyright information in PMC

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