A chemical inhibitor of heat shock protein 78 (HSP78) from <i>Leishmania donovani</i> represents a potential antileishmanial drug candidate.

ABSTRACT: The emergence of resistance to available antileishmanial drugs advocates identification of new drug targets and their inhibitors for visceral leishmaniasis. Here, we identified Leishmania donovani heat shock protein 78 (LdHSP78), a putative caseinolytic protease, as important for parasite infection of host macrophages and a potential therapeutic target. Enrichment of LdHSP78 in infected humans, hamsters, and parasite amastigotes suggested its importance for disease persistence. Heterozygous knockouts of L. donovani HSP78 (LdHSP78+/-) and Leishmania mexicana HSP78 (LmxHSP78+/-) were generated using a flanking UTR-based multifragment ligation strategy and the CRISPR-Cas9 technique, respectively to investigate the significance of HSP78 for disease manifestat

SUBMITTER: Das S 

PROVIDER: S-EPMC7380179 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature