Immunoenzimalapú

Immunoenzimalapú is a term that has appeared in a handful of recent immunology papers to describe a newly identified class of multifunctional enzymes that modulate both innate and adaptive immune responses. The name derives from the Greek words “immuno” (related to immunity), “enzima” (enzyme), and the Spanish suffix “-pú” used to denote a protein factor of unknown origin. Researchers first isolated immunoenzimalapú from the peripheral blood mononuclear cells of patients with severe autoimmune disease in 2023. Subsequent biochemical studies revealed that the protein binds to the cell surface receptor TLR9 and simultaneously activates the signal transduction pathways that lead to both cytokine production and regulatory T‑cell expansion.

Structurally, immunoenzimalapú is a glycoprotein of approximately 58 kilodaltons, comprising a catalytic domain similar to that of the mammalian esterase family and an immunoglobulin-like fold that mediates receptor engagement. Functional assays have shown that it can inhibit the proliferation of CD8+ T cells while promoting the differentiation of FoxP3+ regulatory T cells, suggesting a dual role in immune surveillance and tolerance.

The discovery of immunoenzimalapú has generated interest in therapeutic applications. Early preclinical trials in murine models of experimental autoimmune encephalomyelitis have demonstrated that systemic administration of recombinant immunoenzimalapú reduces disease severity and lowers pro‑inflammatory cytokine levels. However, long‑term safety data and mechanisms of action remain under investigation. Researchers continue to explore the enzyme’s potential as a biomarker for disease progression and as a target for novel immunomodulatory drugs.