ArticlePLoS pathogens2010
Exoerythrocytic Plasmodium parasites secrete a cysteine protease inhibitor involved in sporozoite invasion and capable of blocking cell death of host hepatocytes.
Article in PLoS pathogens, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 71 citations in OpenAlex.
- Discovery of Novel Plasmodium falciparum Pre-Erythrocytic Antigens for Vaccine Development.PloS one · 2015Trial
- Partial characterization of a cysteine protease inhibitor of Plasmodium vivax.Parasites, hosts and diseases · 2025Article
- Morphological characterization, histopathological alteration, and cytokine response of different tissues ofFrontiers in veterinary science · 2025Article
- Therapeutic Targeting and Role of Cysteine Proteases in the Life Cycle of Malaria Parasite.Current medicinal chemistry · 2025Review
- Plasmodium berghei liver stage parasites exploit host GABARAP proteins for TFEB activation.Communications biology · 2024Article
- Roles of Cysteine Proteases in Biology and Pathogenesis of Parasites.Microorganisms · 2023Article
- The origins, isolation, and biological characterization of rodent malaria parasites.Parasitology international · 2022Review
- Inhibitor of Cysteine Protease ofPathogens (Basel, Switzerland) · 2022Article
- A Novel Cysteine Protease Inhibitor ofPathogens (Basel, Switzerland) · 2021Article
- Functional Characterization and Comparison ofMolecular & cellular proteomics : MCP · 2020Article
- Discovery of four new B-cell protective epitopes for malaria using Q beta virus-like particle as platform.NPJ vaccines · 2020Article
- The complex of Plasmodium falciparum falcipain-2 protease with an (E)-chalcone-based inhibitor highlights a novel, small, molecule-binding site.Malaria journal · 2019Article
- Comparing sequence and structure of falcipains and human homologs at prodomain and catalytic active site for malarial peptide based inhibitor design.Malaria journal · 2019Article
- Genetics of Malaria Inflammatory Responses: A Pathogenesis Perspective.Frontiers in immunology · 2019Review
- malERA: An updated research agenda for basic science and enabling technologies in malaria elimination and eradication.PLoS medicine · 2017Review
- Deletion of the rodent malaria ortholog for falcipain-1 highlights differences between hepatic and blood stage merozoites.PLoS pathogens · 2017Article
- Screen of Non-annotated Small Secreted Proteins of Pseudomonas syringae Reveals a Virulence Factor That Inhibits Tomato Immune Proteases.PLoS pathogens · 2016Article
- Assessment ofBiochemistry and biophysics reports · 2016Article
- Ambivalent Outcomes of Cell Apoptosis: A Barrier or Blessing in Malaria Progression.Frontiers in microbiology · 2016Review
- Plasmodium cellular effector mechanisms and the hepatic microenvironment.Frontiers in microbiology · 2015Review
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Plasmodium parasites must control cysteine protease activity that is critical for hepatocyte invasion by sporozoites, liver stage development, host cell survival and merozoite liberation. Here we show that exoerythrocytic P. berghei parasites express a potent cysteine protease inhibitor (PbICP, P. berghei inhibitor of cysteine proteases). We provide evidence that it has an important function in sporozoite invasion and is capable of blocking hepatocyte cell death. Pre-incubation with specific anti-PbICP antiserum significantly decreased the ability of sporozoites to infect hepatocytes and expression of PbICP in mammalian cells protects them against peroxide- and camptothecin-induced cell death. PbICP is secreted by sporozoites prior to and after hepatocyte invasion, localizes to the parasitophorous vacuole as well as to the parasite cytoplasm in the schizont stage and is released into the host cell cytoplasm at the end of the liver stage. Like its homolog falstatin/PfICP in P. falciparum, PbICP consists of a classical N-terminal signal peptide, a long N-terminal extension region and a chagasin-like C-terminal domain. In exoerythrocytic parasites, PbICP is posttranslationally processed, leading to liberation of the C-terminal chagasin-like domain. Biochemical analysis has revealed that both full-length PbICP and the truncated C-terminal domain are very potent inhibitors of cathepsin L-like host and parasite cysteine proteases. The results presented in this study suggest that the inhibitor plays an important role in sporozoite invasion of host cells and in parasite survival during liver stage development by inhibiting host cell proteases involved in programmed cell death.
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