ReviewInfection and immunity2010
Major surface protease of trypanosomatids: one size fits all?
Review in Infection and immunity, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
44 citing papers in PubMed, 104 citations in OpenAlex.
- Autochthonous Leishmaniosis in Dogs, Cats, Horses, and Wildlife in the United States of America.Microorganisms · 2026Review
- Autochthonous Leishmaniasis in the United States of America.Microorganisms · 2025Review
- Exploring the genomic landscape of the GP63 family in Trypanosoma cruzi: Evolutionary dynamics and functional peculiarities.PLoS neglected tropical diseases · 2025Article
- In silico evaluation of N-aryl-1,10-phenanthroline-2-amines as potential inhibitors of T. cruzi GP63 zinc-metalloprotease by docking and molecular dynamics simulations.Scientific reports · 2025Article
- Genetic Diversity and Chromosomal Variations in the IranianAdvanced biomedical research · 2025Article
- Differential expression of peptidases in Strigomonas culicis wild-type and aposymbiotic strains: from proteomic data to proteolytic activity.Memorias do Instituto Oswaldo Cruz · 2024Article
- Leishmania (Sauroleishmania) tarentolae versus pathogenic species: comparative evaluation of protease activity, glycoconjugates, resistance to complement and metabolome composition.Memorias do Instituto Oswaldo Cruz · 2024Article
- Genomes ofPathogens (Basel, Switzerland) · 2023Article
- Promastigote-to-Amastigote Conversion inPathogens (Basel, Switzerland) · 2022Review
- Quantum Biochemistry Screening and In Vitro Evaluation ofInternational journal of molecular sciences · 2022Article
- Differences in Charge Distribution inInternational journal of molecular sciences · 2022Article
- The genomic basis of host and vector specificity in non-pathogenic trypanosomatids.Biology open · 2022Article
- Genetic variation and microbiota in bumble bees cross-infected by different strains of C. bombi.PloS one · 2022Article
- Anti-Leishmania braziliensis activity of 1,10-phenanthroline-5,6-dione and its Cu(II) and Ag(I) complexes.Parasitology research · 2021Article
- Insights intoVeterinary sciences · 2021Review
- Natural Occurrence in Venomous Arthropods of Antimicrobial Peptides Active against Protozoan Parasites.Toxins · 2019Review
- Review
- Article
- Complement Evasion: An Effective Strategy That Parasites Utilize to Survive in the Host.Frontiers in microbiology · 2019Review
- Extracellular release of virulence factor major surface protease via exosomes in Leishmania infantum promastigotes.Parasites & vectors · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Major surface protease (MSP or GP63) is the most abundant glycoprotein localized to the plasma membrane of Leishmania promastigotes. MSP plays several important roles in the pathogenesis of leishmaniasis, including but not limited to (i) evasion of complement-mediated lysis, (ii) facilitation of macrophage (Mø) phagocytosis of promastigotes, (iii) interaction with the extracellular matrix, (iv) inhibition of natural killer cellular functions, (v) resistance to antimicrobial peptide killing, (vi) degradation of Mø and fibroblast cytosolic proteins, and (vii) promotion of survival of intracellular amastigotes. MSP homologues have been found in all other trypanosomatids studied to date including heteroxenous members of Trypanosoma cruzi, the extracellular Trypanosoma brucei, unusual intraerythrocytic Endotrypanum spp., phytoparasitic Phytomonas spp., and numerous monoxenous species. These proteins are likely to perform roles different from those described for Leishmania spp. Multiple MSPs in individual cells may play distinct roles at some time points in trypanosomatid life cycles and collaborative or redundant roles at others. The cellular locations and the extracellular release of MSPs are also discussed in connection with MSP functions in leishmanial promastigotes.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.