ArticleeLife2020
The malaria parasite sheddase SUB2 governs host red blood cell membrane sealing at invasion.
Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 29 citations in OpenAlex.
- Malaria vaccines: Current developments and immunological insights.New microbes and new infections · 2025Article
- Exploring Subtilisin Inhibition to Discover Antimalarial Drugs: Insights into Medicinal Chemistry and Drug Discovery.Pharmaceuticals (Basel, Switzerland) · 2025Review
- Malaria: past, present, and future.Signal transduction and targeted therapy · 2025Review
- A scaleable inducible knockout system for studying essential gene function in the malaria parasite.Nucleic acids research · 2025Article
- Targeting Malaria's Achilles' Heels: A Review of Plasmodium Life Cycle Vulnerabilities for Drug Discovery.Current topics in medicinal chemistry · 2025Review
- Application of optical tweezer technology reveals that PfEBA and PfRH ligands, not PfMSP1, play a central role in Plasmodium falciparum merozoite-erythrocyte attachment.PLoS pathogens · 2024Article
- Post-Translational Modifications of Proteins of Malaria Parasites during the Life Cycle.International journal of molecular sciences · 2024Review
- Plasmepsin X activates the PCRCR complex of Plasmodium falciparum by processing PfRh5 for erythrocyte invasion.Nature communications · 2023Article
- Targeting theHeliyon · 2022Review
- The AMA1-RON complex drives Plasmodium sporozoite invasion in the mosquito and mammalian hosts.PLoS pathogens · 2022Article
- RBC membrane biomechanics and Plasmodium falciparum invasion: probing beyond ligand-receptor interactions.Trends in parasitology · 2022Review
- Protease Inhibition-An Established Strategy to Combat Infectious Diseases.International journal of molecular sciences · 2021Review
- Peptidic boronic acids are potent cell-permeable inhibitors of the malaria parasite egress serine protease SUB1.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Identification of Reticulocyte Binding Domain ofFrontiers in cellular and infection microbiology · 2021Article
- The malaria parasite sheddase SUB2 governs host red blood cell membrane sealing at invasion.eLife · 2020Article
- Actomyosin forces and the energetics of red blood cell invasion by the malaria parasite Plasmodium falciparum.PLoS pathogens · 2020Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Red blood cell (RBC) invasion by malaria merozoites involves formation of a parasitophorous vacuole into which the parasite moves. The vacuole membrane seals and pinches off behind the parasite through an unknown mechanism, enclosing the parasite within the RBC. During invasion, several parasite surface proteins are shed by a membrane-bound protease called SUB2. Here we show that genetic depletion of SUB2 abolishes shedding of a range of parasite proteins, identifying previously unrecognized SUB2 substrates. Interaction of SUB2-null merozoites with RBCs leads to either abortive invasion with rapid RBC lysis, or successful entry but developmental arrest. Selective failure to shed the most abundant SUB2 substrate, MSP1, reduces intracellular replication, whilst conditional ablation of the substrate AMA1 produces host RBC lysis. We conclude that SUB2 activity is critical for host RBC membrane sealing following parasite internalisation and for correct functioning of merozoite surface proteins.
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