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Updated: Oct 29, 2026

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
Published on: October 4, 2017
The fate of cysteine's sulfur in CD8+ T cell function
1Bloomberg-Kimmel Institute of Immunotherapy, Department of Oncology, Johns Hopkins University School of Medicine, Baltimore, MD, USA.
Abstract:
CD8+ T cells modulate their metabolism to support activation, proliferation, and effector function. The sulfur-containing amino acid cysteine is essential for these processes, but beyond its role in protein synthesis, cysteine is metabolized into multiple products that differentially regulate T cell immunity. Here, we review recent advances in understanding how intracellular cysteine routing controls CD8+ T cell function. Cysteine-derived glutathione, iron-sulfur clusters, coenzyme A, hydrogen sulfide, and taurine each have distinct effects on T cell activation, mitochondrial metabolism, and antitumor immunity. Additionally, cysteine-dependent post-translational modifications-including sulfenylation and persulfidation-modulate signaling and gene expression. Understanding how cells balance competing cysteine fates may reveal new therapeutic strategies to enhance T cell responses in cancer and other diseases.
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