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Cysteine proteinase type I, more commonly known as Cysteine proteinase B (CPB), is a critical lysosomal enzyme and major virulence factor found in various species of the protozoan parasite Leishmania, including L. infantum, L. major, and L. braziliensis [1, 4]. It belongs to the papain-like (C1) family of cysteine proteases and is essential for the parasite's survival, replication, and differentiation within host macrophages [3, 8]. CPB facilitates the degradation of host proteins to provide nutrients and plays a key role in modulating the host's immune response to favor parasite persistence [1, 12]. Due to its high immunogenicity and vital role in pathogenesis, CPB is a prominent target for the development of vaccines, including DNA and recombinant protein formulations, as well as small-molecule inhibitors [4, 16]. Therapeutic strategies targeting CPB aim to disrupt its proteolytic activity, thereby impairing parasite viability and promoting a protective Th1-type immune response in the host [1, 10].
Cysteine protease inhibition
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