ArticleThe Journal of biological chemistry2006
The structure of Leishmania mexicana ICP provides evidence for convergent evolution of cysteine peptidase inhibitors.
Article in The Journal of biological chemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 48 citations in OpenAlex.
- Antileishmanial Activity and In Silico Molecular Docking Studies ofTropical medicine and infectious disease · 2023Article
- A novel cysteine protease inhibitor in Baylisascaris schroederi migratory larvae regulates inflammasome activation through the TLR4-ROS-NLRP3 pathway.Parasites & vectors · 2022Article
- Characterization of a novel cysteine protease inhibitor inFrontiers in immunology · 2022Article
- The streptococcal multidomain fibrillar adhesin CshA has an elongated polymeric architecture.The Journal of biological chemistry · 2020Article
- In Silico Analysis of Homologous Heterodimers of Cruzipain-Chagasin from Structural Models Built by Homology.International journal of molecular sciences · 2019Article
- An evaluation of the evolution of the gene structure of dystroglycan.BMC research notes · 2017Article
- Cross-talk between malarial cysteine proteases and falstatin: the BC loop as a hot-spot target.PloS one · 2014Article
- The first structure in a family of peptidase inhibitors reveals an unusual Ig-like fold.F1000Research · 2013Article
- The rust transferred proteins-a new family of effector proteins exhibiting protease inhibitor function.Molecular plant pathology · 2013Article
- The macromolecular complex of ICP and falcipain-2 from Plasmodium: preparation, crystallization and preliminary X-ray diffraction analysis.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
- Exoerythrocytic Plasmodium parasites secrete a cysteine protease inhibitor involved in sporozoite invasion and capable of blocking cell death of host hepatocytes.PLoS pathogens · 2010Article
- Overexpression of the natural inhibitor of cysteine peptidases in Leishmania mexicana leads to reduced virulence and a Th1 response.Infection and immunity · 2009Article
- Ranaspumin-2: structure and function of a surfactant protein from the foam nests of a tropical frog.Biophysical journal · 2009Article
- The cathepsin L of Toxoplasma gondii (TgCPL) and its endogenous macromolecular inhibitor, toxostatin.Molecular and biochemical parasitology · 2009Article
- Structures of falcipain-2 and falcipain-3 bound to small molecule inhibitors: implications for substrate specificity.Journal of medicinal chemistry · 2009Article
- Influence of parasite encoded inhibitors of serine peptidases in early infection of macrophages with Leishmania major.Cellular microbiology · 2009Article
- Identification, characterization of functional candidate genes for host-parasite interactions in entomopathogenetic nematode Steinernema carpocapsae by suppressive subtractive hybridization.Parasitology research · 2008Article
- The role of conserved residues of chagasin in the inhibition of cysteine peptidases.FEBS letters · 2008Article
- Role of the Trypanosoma brucei natural cysteine peptidase inhibitor ICP in differentiation and virulence.Molecular microbiology · 2007Article
- Protein turnover and differentiation in Leishmania.International journal for parasitology · 2007Review
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Authors and funding
6 authors at 2 institutions in 1 country.
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Abstract
Clan CA, family C1 cysteine peptidases (CPs) are important virulence factors and drug targets in parasites that cause neglected diseases. Natural CP inhibitors of the I42 family, known as ICP, occur in some protozoa and bacterial pathogens but are absent from metazoa. They are active against both parasite and mammalian CPs, despite having no sequence similarity with other classes of CP inhibitor. Recent data suggest that Leishmania mexicana ICP plays an important role in host-parasite interactions. We have now solved the structure of ICP from L. mexicana by NMR and shown that it adopts a type of immunoglobulin-like fold not previously reported in lower eukaryotes or bacteria. The structure places three loops containing highly conserved residues at one end of the molecule, one loop being highly mobile. Interaction studies with CPs confirm the importance of these loops for the interaction between ICP and CPs and suggest the mechanism of inhibition. Structure-guided mutagenesis of ICP has revealed that residues in the mobile loop are critical for CP inhibition. Data-driven docking models support the importance of the loops in the ICP-CP interaction. This study provides structural evidence for the convergent evolution from an immunoglobulin fold of CP inhibitors with a cystatin-like mechanism.
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