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Hydrophilic Acylated Surface Protein B (HASPB) is a major surface antigen expressed by Leishmania parasites during their infective stages, specifically metacyclic promastigotes and amastigotes (UniProt P23541). It is characterized by a highly repetitive central domain and undergoes dual acylation (myristoylation and palmitoylation) at the N-terminus, which is essential for its trafficking to the parasite's outer membrane via a non-classical secretion pathway (Denny et al., 2000, J Biol Chem). HASPB plays a vital role in parasite virulence and the establishment of infection within host macrophages (Stegmayer et al., 2005, Traffic). Due to its stage-specific expression and high immunogenicity, it is a leading candidate for the development of vaccines against both visceral and cutaneous leishmaniasis (MacLean et al., 2012, Mol Biochem Parasitol). While no small-molecule inhibitors are currently approved for clinical use, HASPB remains a significant target for immunological interventions and studies into parasite-specific protein export mechanisms (Stijlemans et al., 2016, Expert Rev Vaccines).
Induction of a protective Th1-type immune response characterized by interferon-gamma production; inhibition of parasite surface localization via acylation interference.
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