Leishmania nucleoside hydrolase (NH36) (NH36)

The Leishmania nucleoside hydrolase (NH36) is an enzyme found in all studied species of the Leishmania genus. It catalyzes the hydrolysis of the N-glycosidic bond in ribonucleosides, which is essential because Leishmania parasites cannot synthesize purines de novo and must salvage them from the host. NH36 is a dimeric (or tetrameric) enzyme encoded by a single gene, with high sequence conservation across Leishmania species. It is a validated molecular marker for the genus and a prime target for both anti-Leishmania chemotherapy and vaccine development, as it is the main antigen in vaccines such as Leishmune®. The NH36 enzyme’s structure and surface epitopes have been characterized, and its immunogenic domains stimulate both humoral and cellular immune responses in animal models and humans. While no drugs have reached approval targeting NH36, inhibitors of Leishmania nucleoside hydrolase are in preclinical development as selective, mechanism-based therapeutics. Antibody responses against NH36 serve as markers of infection and efficacy in vaccine studies. Clarification: - The phrase "Leishmania nucleoside hydrolase antigen-specific immune response" in your request refers to the antigen-specific immune response rather than the molecule itself. The best canonical form is the enzyme: "Leishmania nucleoside hydrolase (NH36)." The immune response (T-cell or antibody to NH36) is not the target, but the molecule inducing it is. Thus, the underlying target is NH36 itself.

Other names

nucleoside hydrolase (Leishmania)NH36Leishmania donovani nucleoside hydrolaseLeishmania nucleoside N-ribohydrolase

Inhibitors block the hydrolysis of nucleosides into corresponding bases and ribose, impairing purine salvage