ArticleCellular microbiology2009
Influence of parasite encoded inhibitors of serine peptidases in early infection of macrophages with Leishmania major.
Article in Cellular microbiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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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.
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Who cites it
30 citing papers in PubMed, 49 citations in OpenAlex.
- High-throughput investigation of macromolecular interactions for drug development using spectral shift technology.Biophysical reviews · 2025Review
- Ecotin: A versatile protease inhibitor of bacteria and eukaryotes.Frontiers in microbiology · 2023Review
- Synergy of protease-binding sites within the ecotin homodimer is crucial for inhibition of MASP enzymes and for blocking lectin pathway activation.The Journal of biological chemistry · 2022Article
- Characterization of Differentially Abundant Proteins AmongFrontiers in cellular and infection microbiology · 2022Article
- Role of the inhibitor of serine peptidase 2 (ISP2) of Trypanosoma brucei rhodesiense in parasite virulence and modulation of the inflammatory responses of the host.PLoS neglected tropical diseases · 2021Article
- Kinins and Their Receptors in Infectious Diseases.Pharmaceuticals (Basel, Switzerland) · 2020Review
- Unravelling the proteomic signature of extracellular vesicles released by drug-resistant Leishmania infantum parasites.PLoS neglected tropical diseases · 2020Article
- Characterization of ecotin homologs from Campylobacter rectus and Campylobacter showae.PloS one · 2020Article
- Ecotin, a microbial inhibitor of serine proteases, blocks multiple complement dependent and independent microbicidal activities of human serum.PLoS pathogens · 2019Article
- Neutrophil elastase promotesFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
- Functional genomics in sand fly-derived Leishmania promastigotes.PLoS neglected tropical diseases · 2019Review
- Understanding Leishmania parasites through proteomics and implications for the clinic.Expert review of proteomics · 2018Review
- Inhibitor of serine peptidase 2 enhances Leishmania major survival in the skin through control of monocytes and monocyte-derived cells.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018Article
- Article
- Role of inhibitors of serine peptidases in protecting Leishmania donovani against the hydrolytic peptidases of sand fly midgut.Parasites & vectors · 2017Article
- Metacaspase-binding peptide inhibits heat shock-induced death in Leishmania (L.) amazonensis.Cell death & disease · 2017Article
- Leishmania Infection Engages Non-Receptor Protein Kinases Differentially to Persist in Infected Hosts.Frontiers in immunology · 2016Review
- Role of protein kinase R in the killing of Leishmania major by macrophages in response to neutrophil elastase and TLR4 via TNFα and IFNβ.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2014Article
- Ecotin-like ISP of L. major promastigotes fine-tunes macrophage phagocytosis by limiting the pericellular release of bradykinin from surface-bound kininogens: a survival strategy based on the silencing of proinflammatory G-protein coupled kinin B2 and B1 receptors.Mediators of inflammation · 2014Article
- Patterns of prokaryotic lateral gene transfers affecting parasitic microbial eukaryotes.Genome biology · 2013Article
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
Ecotin is a potent inhibitor of family S1A serine peptidases, enzymes lacking in the protozoan parasite Leishmania major. Nevertheless, L. major has three ecotin-like genes, termed inhibitor of serine peptidase (ISP). ISP1 is expressed in vector-borne procyclic and metacyclic promastigotes, whereas ISP2 is also expressed in the mammalian amastigote stage. Recombinant ISP2 inhibited neutrophil elastase, trypsin and chymotrypsin with K(i)s between 7.7 and 83 nM. L. major ISP2-ISP3 double null mutants (Deltaisp2/3) were created. These grew normally as promastigotes, but were internalized by macrophages more efficiently than wild-type parasites due to the upregulation of phagocytosis by a mechanism dependent on serine peptidase activity. Deltaisp2/3 promastigotes transformed to amastigotes, but failed to divide for 48 h. Intracellular multiplication of Deltaisp2/3 was similar to wild-type parasites when serine peptidase inhibitors were present, suggesting that defective intracellular growth results from the lack of serine peptidase inhibition during promastigote uptake. Deltaisp2/3 mutants were more infective than wild-type parasites to BALB/c mice at the early stages of infection, but became equivalent as the infection progressed. These data support the hypothesis that ISPs of L. major target host serine peptidases and influence the early stages of infection of the mammalian host.
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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.