ArticleCell stress & chaperones2015
Leishmania donovani P23 protects parasites against HSP90 inhibitor-mediated growth arrest.
Article in Cell stress & chaperones, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 17 citations in OpenAlex.
- Whole genome sequencing reveals genomic diversity and evidence of hybridization in MoroccanFrontiers in cellular and infection microbiology · 2026Article
- Review
- The pathogenicity and virulence of Leishmania - interplay of virulence factors with host defenses.Virulence · 2022Review
- Nanodiagnostics in leishmaniasis: A new frontiers for early elimination.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology · 2021Review
- Novel Small Molecule Hsp90/Cdc37 Interface Inhibitors Indirectly Target K-Ras-Signaling.Cancers · 2021Article
- Heat Shock Proteins as the Druggable Targets in Leishmaniasis: Promises and Perils.Infection and immunity · 2021Review
- Casein kinase 1.2 over expression restores stress resistance to Leishmania donovani HSP23 null mutants.Scientific reports · 2020Article
- Small Molecule Inhibitors Targeting the Heat Shock Protein System of Human Obligate Protozoan Parasites.International journal of molecular sciences · 2019Review
- Leishmania donovani 90 kD Heat Shock Protein - Impact of Phosphosites on Parasite Fitness, Infectivity and Casein Kinase Affinity.Scientific reports · 2019Article
- Article
- Hsp90 inhibitors radicicol and geldanamycin have opposing effects on Leishmania Aha1-dependent proliferation.Cell stress & chaperones · 2017Article
- The HSP90 chaperone machinery.Nature reviews. Molecular cell biology · 2017Review
- The heat shock protein 90 of Toxoplasma gondii is essential for invasion of host cells and tachyzoite growth.Parasite (Paris, France) · 2017Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In Leishmania donovani, the HSP90 chaperone complex plays an essential role in the control of the parasite's life cycle, general viability and infectivity. Several of the associated co-chaperones were also shown to be essential for viability and/or infectivity to mammalian cells. Here, we identify and describe the co-chaperone P23 and distinguish its function from that of the structurally related small heat shock protein HSP23. P23 is expressed constitutively and associates itself with members of the HSP90 complex, i.e. HSP90 and Sti1. Viable P23 gene replacement mutants could be raised and confirmed as null mutants without deleterious effects on viability under a variety of physiological growth conditions. The null mutant also displays near-wild-type infectivity, arguing against a decisive role played by P23 in laboratory settings. However, the P23 null mutant displays a marked hypersensitivity against HSP90 inhibitors geldanamycin and radicicol. P23 also appears to affect the radicicol resistance of a HSP90 Leu33-Ile mutant described previously. Therefore, the annotation of L. donovani P23 as HSP90-interacting co-chaperone is confirmed.
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