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Background：
Lysine pyruvylation is a novel type of protein post-translational modification first identified in 2026. Pyruvate is an intermediate metabolite of glycolysis. Hyperglycemic conditions or aberrant activation of glycolysis lead to pyruvate accumulation, which can undergo nucleophilic addition reaction with lysine residues. Recent research advances have revealed that serum pyruvate levels are elevated in hyperglycemic individuals, accompanied by increased lysine pyruvylation of STAT1. This modification markedly reduces the expression of interferon-stimulated genes (ISGs), thereby impairing type I interferon (IFN-I)-mediated antiviral immune responses and further increasing susceptibility to viral infections in hyperglycemic populations. Meanwhile, this study provides a novel strategy to restore the therapeutic efficacy of IFN-I-based antiviral therapy in individuals with elevated blood glucose. Additionally, lysine pyruvylation may exert crucial regulatory roles in tumor metabolism, inflammation, immune disorders and other related research fields.
