ArticleMemorias do Instituto Oswaldo Cruz2019
Calpains of Leishmania braziliensis: genome analysis, differential expression, and functional analysis.
Article in Memorias do Instituto Oswaldo Cruz, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 16 citations in OpenAlex.
- PluronicInternational journal of molecular sciences · 2026Article
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- An inclusive assessment of apoptosis mechanisms inCurrent research in parasitology & vector-borne diseases · 2025Review
- Susceptibility ofTropical medicine and infectious disease · 2024Article
- Characterization of the Effect ofInternational journal of molecular sciences · 2024Article
- Differential expression of peptidases in Strigomonas culicis wild-type and aposymbiotic strains: from proteomic data to proteolytic activity.Memorias do Instituto Oswaldo Cruz · 2024Article
- Assessing proteases and enzymes of the trypanothione system in subpopulations of Leishmania (Viannia) braziliensis Thor strain during macrophage infection.Memorias do Instituto Oswaldo Cruz · 2024Article
- Membrane-anchored calpains - hidden regulators of growth and development beyond plants?Frontiers in plant science · 2023Article
- Subtilisin ofCurrent issues in molecular biology · 2022Article
- Antileishmanial Efficacy of the Calpain Inhibitor MDL28170 in Combination with Amphotericin B.Tropical medicine and infectious disease · 2022Article
- Proteolytic inhibitors as alternative medicines to treat trypanosomatid-caused diseases: experience with calpain inhibitors.Memorias do Instituto Oswaldo Cruz · 2022Article
- Novel Insights IntoFrontiers in cellular and infection microbiology · 2022Article
- Serine proteases profiles of Leishmania (Viannia) braziliensis clinical isolates with distinct susceptibilities to antimony.Scientific reports · 2021Article
- The Diverse Calpain Family in Trypanosomatidae: Functional Proteins Devoid of Proteolytic Activity?Cells · 2021Review
- Expression and cellular localisation of Trypanosoma cruzi calpains.Memorias do Instituto Oswaldo Cruz · 2020Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundCalpains are proteins belonging to the multi-gene family of calcium-dependent cysteine peptidases that undergo tight on/off regulation, and uncontrolled proteolysis of calpains is associated with severe human pathologies. Calpain orthologues are expanded and diversified in the trypanosomatids genome.
objectivesHere, we characterised calpains in Leishmania braziliensis, the main causative agent of cutaneous leishmaniasis in Brazil. METHODS/
findingsIn total, 34 predicted calpain-like genes were identified. After domain structure evaluation, reverse transcription-quantitative polymerase chain reaction (RT-qPCR) during in vitro metacyclogenesis revealed (i) five genes with enhanced expression in the procyclic stage, (ii) one augmented gene in the metacyclic stage, and (iii) one procyclic-exclusive transcript. Western blot analysis revealed that an antibody against a consensus-conserved peptide reacted with multiple calpain-like proteins, which is consistent with the multi-gene family characteristic. Flow cytometry and immunocytochemistry analyses revealed the presence of calpain-like molecules mainly in the cytoplasm, to a lesser extent in the plasma membrane, and negligible levels in the nucleus, which are all consistent with calpain localisation. Eventually, the calpain inhibitor MDL28170 was used for functional studies revealing (i) a leishmaniostatic effect, (ii) a reduction in the association index in mouse macrophages, (iii) ultra-structural alterations conceivable with autophagy, and (iv) an enhanced expression of the virulence factor GP63.
conclusionThis report adds novel insights into the domain structure, expression, and localisation of L. braziliensis calpain-like molecules.
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