ArticleMolecular and biochemical parasitology2009
Plasmodium falciparum merozoite surface protein 2 is unstructured and forms amyloid-like fibrils.
Article in Molecular and biochemical parasitology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
48 citing papers in PubMed, 87 citations in OpenAlex.
- A Library of Plasmodium vivax Recombinant Merozoite Proteins Reveals New Vaccine Candidates and Protein-Protein Interactions.PLoS neglected tropical diseases · 2015Trial
- An abundant merozoite surface protein ofeLife · 2026Article
- Non-Vesicular Extracellular Particle (NVEP) Proteomes from Diverse Biological Sources Reveal Specific Marker Composition with Varying Enrichment Levels.Biomolecules · 2025Article
- Malaria: past, present, and future.Signal transduction and targeted therapy · 2025Review
- Apicoplast-derived isoprenoids are essential for biosynthesis of GPI protein anchors, and consequently for egress and invasion in Plasmodium falciparum.PLoS pathogens · 2024Article
- Naturally acquired IgG responses toFrontiers in immunology · 2024Article
- Characterization of a novelFrontiers in immunology · 2023Article
- Uncovering the universality of self-replication in protein aggregation and its link to disease.Science advances · 2022Article
- Guiding the Immune Response to a Conserved Epitope in MSP2, an Intrinsically Disordered Malaria Vaccine Candidate.Vaccines · 2021Article
- Asparaginyl endopeptidases: enzymology, applications and limitations.Organic & biomolecular chemistry · 2021Review
- Amyloids: The History of Toxicity and Functionality.Biology · 2021Review
- Inclusion of an OptimizedJournal of immunology (Baltimore, Md. : 1950) · 2021Article
- Functional Amyloids Are the Rule Rather Than the Exception in Cellular Biology.Microorganisms · 2020Review
- Detection of Protein Aggregation in LiveAntimicrobial agents and chemotherapy · 2020Article
- A suite of kinetically superior AEP ligases can cyclise an intrinsically disordered protein.Scientific reports · 2019Article
- Immunization with merozoite surface protein 2 fused to a Plasmodium-specific carrier protein elicits strain-specific and strain-transcending, opsonizing antibody.Scientific reports · 2019Article
- Microbial functional amyloids serve diverse purposes for structure, adhesion and defence.Biophysical reviews · 2019Review
- Modulation of the aggregation of an amyloidogenic sequence by flanking-disordered region in the intrinsically disordered antigen merozoite surface protein 2.European biophysics journal : EBJ · 2019Article
- Disordered epitopes as peptide vaccines.Peptide science (Hoboken, N.J.) · 2018Review
- The Physiological and Pathological Implications of the Formation of Hydrogels, with a Specific Focus on Amyloid Polypeptides.Biomolecules · 2017Review
Corrections and comments
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Authors and funding
13 authors at 5 institutions in 1 country.
Funding
Abstract
Several merozoite surface proteins are being assessed as potential components of a vaccine against Plasmodium falciparum, the cause of the most serious form of human malaria. One of these proteins, merozoite surface protein 2 (MSP2), is unusually hydrophilic and contains tandem sequence repeats, characteristics of intrinsically unstructured proteins. A range of physicochemical studies has confirmed that recombinant forms of MSP2 are largely unstructured. Both dimorphic types of MSP2 (3D7 and FC27) are equivalently extended in solution and form amyloid-like fibrils although with different kinetics and structural characteristics. These fibrils have a regular underlying beta-sheet structure and both fibril types stain with Congo Red, but only the FC27 fibrils stain with Thioflavin T. 3D7 MSP2 fibrils seeded the growth of fibrils from 3D7 or FC27 MSP2 monomer indicating the involvement of a conserved region of MSP2 in fibril formation. Consistent with this, digestion of fibrils with proteinase K generated resistant peptides, which included the N-terminal conserved region of MSP2. A monoclonal antibody that reacted preferentially with monomeric recombinant MSP2 did not react with the antigen in situ on the merozoite surface. Glutaraldehyde cross-linking of infected erythrocytes generated MSP2 oligomers similar to those formed by polymeric recombinant MSP2. We conclude that MSP2 oligomers containing intermolecular beta-strand interactions similar to those in amyloid fibrils may be a component of the fibrillar surface coat on P. falciparum merozoites.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.