ArticleJournal of cell science2014
A small heat shock protein is essential for thermotolerance and intracellular survival of Leishmania donovani.
Article in Journal of cell science, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 58 citations in OpenAlex.
- Essential role of glycogen synthase kinase 3 in regulating growth, drug response, and infectivity inAntimicrobial agents and chemotherapy · 2026Article
- Biochemistry of Heat Shock Proteins From Human Intracellular Protozoan Parasites as Diagnostic and Therapeutic Biomarkers.Biochemistry · 2025Review
- Molecular, structural, and functional characterization of delta subunit of T-complex protein-1 fromInfection and immunity · 2024Article
- Intraperitoneal Administration of 17-DMAG as an Effective Treatment againstPathogens (Basel, Switzerland) · 2024Article
- Integrative analysis of genome and transcriptome reveal the genetic basis of high temperature tolerance in pleurotus giganteus (Berk. Karun & Hyde).BMC genomics · 2023Article
- The pathogenicity and virulence of Leishmania - interplay of virulence factors with host defenses.Virulence · 2022Review
- Promastigote-to-Amastigote Conversion inPathogens (Basel, Switzerland) · 2022Review
- Global distribution of treatment resistance gene markers for leishmaniasis.Journal of clinical laboratory analysis · 2022Review
- Unraveling of interacting protein network of chaperonin TCP1 gamma subunit of Leishmania donovani.Cell stress & chaperones · 2022Article
- Haploid Genome Analysis Reveals a Tandem Cluster of FourMicrobiology spectrum · 2021Article
- Life Cycle Stage-Specific Accessibility of Leishmania donovani Chromatin at Transcription Start Regions.mSystems · 2021Article
- Insights intoVeterinary sciences · 2021Review
- Proteomic analysis reveals differentially abundant proteins probably involved in the virulence of amastigote and promastigote forms of Leishmania infantum.Parasitology research · 2021Article
- Heat Shock Proteins as the Druggable Targets in Leishmaniasis: Promises and Perils.Infection and immunity · 2021Review
- Development and Characterization of PLGA Nanoparticles Containing 17-DMAG, an Hsp90 Inhibitor.Frontiers in chemistry · 2021Article
- TheGenes · 2020Article
- Article
- Casein kinase 1.2 over expression restores stress resistance to Leishmania donovani HSP23 null mutants.Scientific reports · 2020Article
- A chemical inhibitor of heat shock protein 78 (HSP78) fromThe Journal of biological chemistry · 2020Article
- Article
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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
Leishmania parasites must survive and proliferate in two vastly different environments - the guts of poikilothermic sandflies and the antigen-presenting cells of homeothermic mammals. The change of temperature during the transmission from sandflies to mammals is both a key trigger for the progression of their life cycle and for elevated synthesis of heat shock proteins, which have been implicated in their survival at higher temperatures. Although the functions of the main heat shock protein families in the Leishmania life cycle have been studied, nothing is known about the roles played by small heat shock proteins. Here, we present the first evidence for the pivotal role played by the Leishmania donovani 23-kDa heat shock protein (which we called HSP23), which is expressed preferentially during the mammalian stage where it assumes a perinuclear localisation. Loss of HSP23 causes increased sensitivity to chemical stressors and renders L. donovani non-viable at 37°C. Consequently, HSP23-null mutants are non-infectious to primary macrophages in vitro. All phenotypic effects could be abrogated by the introduction of a functional HSP23 transgene into the null mutant, confirming the specificity of the mutant phenotype. Thus, HSP23 expression is a prerequisite for L. donovani survival at mammalian host temperatures and a crucial virulence factor.
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