ArticlePLoS pathogens2011
Plasmodium protease ROM1 is important for proper formation of the parasitophorous vacuole.
Article in PLoS pathogens, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 32 citations in OpenAlex.
- Rhomboid Proteases in Plasmodium spp. : Biology, Functional Roles, and Therapeutic Potential.Acta parasitologica · 2026Review
- Identification of two genomic cryptotypes of Plasmodium malariae in Africa.PLoS neglected tropical diseases · 2026Article
- Two Plasmodium vivax hypnozoite-expressed RNA-binding proteins inhibit liver stage replication.Nature communications · 2026Article
- TEpiNom: A computational framework integrating population data to prioritize Plasmodium falciparum T cell epitopes.Vaccine · 2026Article
- TwoResearch square · 2025Article
- Post-Translational Modifications of Proteins of Malaria Parasites during the Life Cycle.International journal of molecular sciences · 2024Review
- Hijacking the human complement inhibitor C4b-binding protein by the sporozoite stage of theFrontiers in immunology · 2022Article
- Sickle Cell Trait Modulates the Proteome and Phosphoproteome ofFrontiers in cellular and infection microbiology · 2021Article
- Plasmodium vivax rhomboid-like protease 1 gene diversity in Thailand.Experimental parasitology · 2017Article
- Proteases as antimalarial targets: strategies for genetic, chemical, and therapeutic validation.The FEBS journal · 2017Review
- Cryptosporidium parvum rhomboid1 has an activity in microneme protein CpGP900 cleavage.Parasites & vectors · 2016Article
- Article
- A Trichomonas vaginalis Rhomboid Protease and Its Substrate Modulate Parasite Attachment and Cytolysis of Host Cells.PLoS pathogens · 2015Article
- Entamoeba histolytica rhomboid protease 1 has a role in migration and motility as validated by two independent genetic approaches.Experimental parasitology · 2015Article
- Serine Proteases of Malaria Parasite Plasmodium falciparum: Potential as Antimalarial Drug Targets.Interdisciplinary perspectives on infectious diseases · 2014Review
- The roles of intramembrane proteases in protozoan parasites.Biochimica et biophysica acta · 2013Review
- Torins are potent antimalarials that block replenishment of Plasmodium liver stage parasitophorous vacuole membrane proteins.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Total and putative surface proteomics of malaria parasite salivary gland sporozoites.Molecular & cellular proteomics : MCP · 2013Article
- Pre-erythrocytic malaria vaccines: identifying the targets.Expert review of vaccines · 2012Review
- Malaria parasite pre-erythrocytic infection: preparation meets opportunity.Cellular microbiology · 2012Review
Corrections and comments
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Authors and funding
4 authors at 4 institutions in 1 country.
Funding
Abstract
Apicomplexans are obligate intracellular parasites that invade host cells by an active process leading to the formation of a non-fusogenic parasitophorous vacuole (PV) where the parasite replicates within the host cell. The rhomboid family of proteases cleaves substrates within their transmembrane domains and has been implicated in the invasion process. Although its exact function is unknown, Plasmodium ROM1 is hypothesized to play a role during invasion based on its microneme localization and its ability to cleave essential invasion adhesins. Using the rodent malaria model, Plasmodium yoelii, we carried out detailed quantitative analysis of pyrom1 deficient parasites during the Plasmodium lifecycle. Pyrom1(-) parasites are attenuated during erythrocytic and hepatic stages but progress normally through the mosquito vector with normal counts of oocyst and salivary gland sporozoites. Pyrom1 steady state mRNA levels are upregulated 20-fold in salivary gland sporozoites compared to blood stages. We show that pyrom1(-) sporozoites are capable of gliding motility and traversing host cells normally. Wildtype and pyrom1(-) sporozoites do not differ in the rate of entry into Hepa1-6 hepatocytes. Within the first twelve hours of hepatic development, however, only 50% pyrom1(-) parasites have developed into exoerythrocytic forms. Immunofluorescence microscopy using the PVM marker UIS4 and transmission electron microscopy reveal that the PV of a significant fraction of pyrom1(-) parasites are morphologically aberrant shortly after invasion. We propose a novel function for PyROM1 as a protease that promotes proper PV modification to allow parasite development and replication in a suitable environment within the mammalian host.
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