ArticleNature communications2017
Protein O-fucosylation in Plasmodium falciparum ensures efficient infection of mosquito and vertebrate hosts.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed.
- RTS,S/AS02A Malaria Vaccine-Induced IgG Responses Equally Recognize Native-Like Fucosylated and Nonfucosylated Plasmodium falciparum Circumsporozoite Proteins.The Journal of infectious diseases · 2024Trial
- Crystal structure of a β1,3-Glucosyltransferase reveals an unusual substrate recognition by a two-domain GT-A fold glycosyltransferase.The Journal of biological chemistry · 2026Article
- The long and winding road: On the endoplasmic reticulum of Plasmodium and implications for pathogenesis.PLoS pathogens · 2026Review
- Investigation of carbohydrate-based molecules ofFrontiers in veterinary science · 2026Article
- Structure, function, and implications of fucosyltransferases in health and disease.Nature communications · 2025Review
- CSP ubiquitylation favours Plasmodium berghei survival during early liver stage infection.Scientific reports · 2025Article
- The Plasmodium circumsporozoite protein.Trends in parasitology · 2024Review
- Flp/Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Post-Translational Modifications of Proteins of Malaria Parasites during the Life Cycle.International journal of molecular sciences · 2024Review
- Glycosylation in malaria parasites: what do we know?Trends in parasitology · 2024Review
- Rhoptry neck protein 4 plays important roles duringmSphere · 2023Article
- Conservation, abundance, glycosylation profile, and localization of the TSP protein family in Cryptosporidium parvum.The Journal of biological chemistry · 2023Article
- Tryptophan C-mannosylation is critical for Plasmodium falciparum transmission.Nature communications · 2022Article
- Dual Transcriptomics To Determine Gamma Interferon-Independent Host Response to Intestinal Cryptosporidium parvum Infection.Infection and immunity · 2022Article
- Enzymatic and structural characterization of HAD5, an essential phosphomannomutase of malaria-causing parasites.The Journal of biological chemistry · 2022Article
- SialylatedJournal of extracellular biology · 2022Article
- Thrombospondin Related Anonymous Protein Superfamily in Vector-Borne Apicomplexans: The Parasite's Toolkit for Cell Invasion.Frontiers in cellular and infection microbiology · 2022Review
- Isoprenoid alcohols utilization by malaria parasites.Frontiers in chemistry · 2022Article
- Compounds targeting GPI biosynthesis orComputational and structural biotechnology journal · 2022Article
- Cognizance of posttranslational modifications in vaccines: A way to enhanced immunogenicity.Journal of cellular physiology · 2021Review
Corrections and comments
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Authors and funding
14 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
O-glycosylation of the Plasmodium sporozoite surface proteins CSP and TRAP was recently identified, but the role of this modification in the parasite life cycle and its relevance to vaccine design remain unclear. Here, we identify the Plasmodium protein O-fucosyltransferase (POFUT2) responsible for O-glycosylating CSP and TRAP. Genetic disruption of POFUT2 in Plasmodium falciparum results in ookinetes that are attenuated for colonizing the mosquito midgut, an essential step in malaria transmission. Some POFUT2-deficient parasites mature into salivary gland sporozoites although they are impaired for gliding motility, cell traversal, hepatocyte invasion, and production of exoerythrocytic forms in humanized chimeric liver mice. These defects can be attributed to destabilization and incorrect trafficking of proteins bearing thrombospondin repeats (TSRs). Therefore, POFUT2 plays a similar role in malaria parasites to that in metazoans: it ensures the trafficking of Plasmodium TSR proteins as part of a non-canonical glycosylation-dependent endoplasmic reticulum protein quality control mechanism.The role of O-glycosylation in the malaria life cycle is largely unknown. Here, the authors identify a Plasmodium protein O-fucosyltransferase and show that it is important for normal trafficking of a subset of surface proteins, particularly CSP and TRAP, and efficient infection of mosquito and vertebrate hosts.
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