Affinage · Plasmodium

CyRPA

PF3D7_0423800 · cysteine-rich protective antigen

Annotated
2026-09-07
65 papers in source corpus 16 papers cited in narrative 16 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

CyRPA (PF3D7_0423800) is a GPI-anchored, apically localized micronemal protein of the P. falciparum merozoite that is essential for erythrocyte invasion, acting as the central structural scaffold of the PfRH5–PfRIPR–CyRPA (RCR) tripartite complex and the larger PCRCR pentameric complex (PMID:25583518, PMID:27374406, PMID:36396942). Structurally it is a six-bladed β-propeller resembling a sialidase fold but is enzymatically inert, fulfilling a purely non-enzymatic role (PMID:28195038). CyRPA mediates assembly of the invasion complex: it binds PfRH5 directly and contacts both PfRH5 and PfRIPR through blades 4–6 of the propeller, presenting PfRH5 within the structured core while the PfRIPR tail extends flexibly, and the assembled complex binds erythrocytes far more efficiently than PfRH5 alone (PMID:28195530, PMID:30542156, PMID:38123677). During invasion CyRPA colocalizes with PfRH5 and PfRIPR at the merozoite–erythrocyte tight junction, where the complex triggers host Ca2+ release and anchors membrane contact; complex function is activated by plasmepsin X processing of PfRH5's prodomain in micronemes (PMID:27374406, PMID:36396942, PMID:37072430). Independently of its scaffolding role, CyRPA acts as a lectin that binds erythrocyte glycans terminating in human α2-6-linked Neu5Ac, with point mutations in the lectin site impairing invasion (PMID:38573856). CyRPA is a leading blood-stage vaccine target: growth-inhibitory antibodies cluster on one face of the propeller (blades 1–2), neutralizing invasion by blocking complex formation or through steric occlusion, and act synergistically both in pairs and in combination with anti-PfRH5 antibodies (PMID:28195530, PMID:30965383, PMID:38123677, PMID:35177602). Notably, the CyRPA ortholog in P. knowlesi is likewise essential for invasion but functions independently, without forming a complex with a PfRIPR or PfRH5 counterpart (PMID:31185066).

Mechanistic history

Synthesis pass · year-by-year structured walk · 12 steps
  1. 2012 Medium

    Established that CyRPA is an invasion-relevant antigen by showing apical expression in schizonts/merozoites and that specific antibodies block parasite growth in vitro and in humanized mice.

    Evidence Immunofluorescence, in vitro growth inhibition, and passive immunization in a humanized mouse model

    PMID:22593616

    Open questions at the time
    • No molecular partners or mechanism of invasion contribution identified
    • Whether CyRPA acts alone or in a complex not addressed
  2. 2015 High

    Resolved how CyRPA contributes to invasion by showing it is a GPI-anchored micronemal protein that assembles with PfRH5 and PfRIPR into an essential complex, and does not bind erythrocytes directly — explaining that its inhibitory antibodies act by blocking complex interactions.

    Evidence GPI-anchor biochemistry, reciprocal co-immunoprecipitation, conditional knockdown, and growth inhibition assays

    PMID:25583518

    Open questions at the time
    • Structural basis of the interactions unknown
    • Direct erythrocyte-binding role (later revised by lectin activity) not yet examined
  3. 2016 High

    Placed the complex at the point of entry by showing CyRPA colocalizes with PfRH5/PfRIPR at the tight junction and is required to trigger host Ca2+ release, defining the functional step it controls during invasion.

    Evidence Conditional loss-of-function, super-resolution microscopy, and Ca2+ release assay

    PMID:27374406

    Open questions at the time
    • Molecular trigger of Ca2+ release not defined
    • CyRPA's specific contribution versus the whole complex not isolated
  4. 2017 High

    Defined CyRPA's molecular nature and the antibody target by solving its six-bladed β-propeller structure, ruling out sialidase activity, mapping the PfRH5-interacting region, and showing an inhibitory antibody blocks CyRPA–PfRH5 binding and complex formation.

    Evidence X-ray crystallography of free CyRPA and CyRPA–Fab complexes, sialidase activity assay (negative), direct PfRH5-binding and antibody-blocking assays

    PMID:28195038 PMID:28195530

    Open questions at the time
    • Architecture of the full trimeric complex not resolved
    • Role of remaining propeller faces unknown
  5. 2018 High

    Revealed the architecture of the assembled RCR complex, showing CyRPA uses blades 4–6 to bridge PfRH5 and PfRIPR and that the complex enhances erythrocyte binding over PfRH5 alone, defining CyRPA as the assembly hub.

    Evidence Subnanometre cryo-EM structure of the Rh5–CyRPA–Ripr complex plus erythrocyte binding assay

    PMID:30542156

    Open questions at the time
    • Dynamics of proposed complex dissociation during membrane insertion not directly observed
    • Precise contribution of each blade contact to invasion untested
  6. 2019 Medium

    Confirmed the antibody neutralization mechanism by directly demonstrating that anti-CyRPA antibodies prevent trimeric complex formation.

    Evidence Antibody blocking of complex assembly plus growth inhibition assay

    PMID:30965383

    Open questions at the time
    • Does not distinguish assembly blockade from steric mechanisms
    • Epitope face not mapped in this study
  7. 2019 Medium

    Tested conservation of CyRPA function across species, showing P. knowlesi CyRPA is essential for invasion but functions without forming a PfRIPR/PfRH5-like complex, indicating the complex-dependent mechanism is not universal.

    Evidence Conditional knockdown in P. knowlesi and co-immunoprecipitation (negative for complex)

    PMID:31185066

    Open questions at the time
    • Mechanism by which PkCyRPA acts independently unknown
    • PkCyRPA binding partners not identified
  8. 2022 Medium

    Extended the complex to a pentameric PCRCR assembly (PfPTRAMP, PfCSS, PfRH5, PfRIPR, CyRPA) that anchors merozoite–erythrocyte membrane contact during deformation, and defined the CyRPA epitope face driving synergistic antibody neutralization.

    Evidence Conditional knockouts, invasion-inhibitory nanobodies, lattice light-sheet microscopy, complex biochemistry (PCRCR); structural studies, SPR kinetics and combination GIA (antibody synergy)

    PMID:35177602 PMID:36396942

    Open questions at the time
    • CyRPA's specific role within PCRCR not separated from the whole complex
    • In vivo relevance of antibody synergy not established
  9. 2023 High

    Clarified regulation and mechanism by showing plasmepsin X processing of PfRH5 activates the PCRCR complex to bind basigin, resolving the full RCR structure with CyRPA presenting PfRH5, and demonstrating anti-CyRPA antibodies inhibit both by steric occlusion and by prematurely inactivating extracellular merozoites.

    Evidence Conditional PMX knockdown and processing/binding assays; cryo-EM of the full PfRCR complex with modelling; live-cell imaging with mAbs

    PMID:37072430 PMID:37713419 PMID:38123677

    Open questions at the time
    • How processing propagates to CyRPA function not directly tested
    • Mechanism of premature merozoite inactivation unknown
  10. 2024 High

    Revised the view that CyRPA does not engage erythrocytes by identifying it as a lectin binding human α2-6-linked Neu5Ac, with lectin-site point mutations impairing invasion, assigning CyRPA a direct receptor-recognition function.

    Evidence Glycan-binding assays, molecular modelling, site-directed mutagenesis in endogenous transgenic parasites, and functional invasion/GIA assays

    PMID:38573856

    Open questions at the time
    • Reconciliation with earlier finding that CyRPA does not bind erythrocytes directly not fully resolved
    • How lectin binding integrates with complex assembly during invasion unclear
  11. 2026 Medium

    Advanced CyRPA as a vaccine immunogen by showing a structure-guided blades 1–2 epitope mimic elicits superior growth-inhibitory antibodies, confirming these blades harbour the critical protective epitopes.

    Evidence Structure-guided protein engineering, preclinical immunization, and growth inhibition assay

    PMID:41772083

    Open questions at the time
    • Efficacy in humans not established
    • Durability and breadth of the antibody response not addressed
  12. 2025 Low

    Examined the evolutionary origin of CyRPA's human glycan specificity, finding that lectin-site residues 154 and 209 are identical between P. falciparum and its gorilla precursor P. praefalciparum, so these sites do not explain adaptation to human erythrocytes.

    Evidence Comparative genome sequence analysis across P. falciparum, P. praefalciparum, and P. reichenowi

    PMID:39865504

    Open questions at the time
    • Purely computational; no experimental test of glycan preference for the precursor CyRPA
    • Actual determinants of host adaptation remain unidentified

Open questions

Synthesis pass · forward-looking unresolved questions
  • How CyRPA's lectin-mediated sialoglycan binding is mechanistically integrated with its scaffolding of the RCR/PCRCR complex, PfRH5 presentation, and the triggering of host Ca2+ release during tight-junction formation remains to be defined.
  • Temporal and spatial coordination of lectin binding versus complex assembly unknown
  • Molecular link from complex engagement to erythrocyte Ca2+ release undefined
  • CyRPA's autonomous contribution within the pentameric PCRCR not experimentally isolated

Mechanism profile

Synthesis pass · controlled-vocabulary classification
Partners
ERYTHROCYTE Α2-6-LINKED NEU5AC SIALOGLYCANS (LIGAND)PFCSS (VIA PCRCR COMPLEX)PFPTRAMP (VIA PCRCR COMPLEX)PFRH5PFRIPRPLASMEPSIN X (REGULATES COMPLEX VIA PFRH5 PROCESSING)
Complex memberships
PCRCR pentameric complex (PfPTRAMP, PfCSS, PfRH5, PfRIPR, CyRPA)PfRH5–CyRPA–PfRIPR (RCR) tripartite complex

Evidence

Reading pass · 16 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2012 CyRPA is expressed in late schizonts, localizes at the apex of merozoites by immunofluorescence, and CyRPA-specific monoclonal antibodies substantially inhibit parasite growth in vitro and in vivo in a P. falciparum NOD-scid IL2Rγ(null) mouse model engrafted with human erythrocytes, establishing a role for CyRPA in erythrocyte invasion. Immunofluorescence microscopy; in vitro growth inhibition assay; passive immunization in humanized mouse model Journal of immunology Medium 22593616
2015 CyRPA is a GPI-anchored protein that localizes in the micronemes and forms a multiprotein complex with PfRH5 and PfRipr on the merozoite surface; co-immunoprecipitation with antibodies against each of the three proteins detected the intact complex; CyRPA is essential for erythrocyte invasion; CyRPA does not bind erythrocytes directly, indicating its invasion-inhibitory antibodies likely act by blocking PfRH5-PfRipr/CyRPA interactions; antibodies against CyRPA and PfRH5 showed synergistic invasion inhibition. GPI-anchor verification; immunofluorescence/co-localization; co-immunoprecipitation; conditional knockdown; in vitro growth inhibition assay Proceedings of the National Academy of Sciences of the United States of America High 25583518
2016 Conditional loss of CyRPA function blocks merozoite invasion of erythrocytes; super-resolution microscopy showed CyRPA colocalizes with PfRipr and PfRH5 at the junction between merozoites and erythrocytes during invasion; the PfRH5/PfRipr/CyRPA complex is required for triggering Ca2+ release from the host erythrocyte and establishing the tight junction. Conditional expression system (loss-of-function); super-resolution microscopy; Ca2+ release assay Cell host & microbe High 27374406
2017 Crystal structure of CyRPA reveals a six-bladed β-propeller fold similar to the sialidase fold, but CyRPA has no sialidase activity and fulfills a purely non-enzymatic structural function; crystal structure of CyRPA in complex with an invasion-inhibitory antibody Fab fragment identifies the protective antibody epitope. X-ray crystallography (CyRPA alone and CyRPA-Fab complex); sialidase activity assay (negative result for enzymatic activity) eLife High 28195038
2017 CyRPA directly interacts with PfRH5; an invasion-inhibitory monoclonal antibody to CyRPA blocks CyRPA binding to PfRH5 and prevents complex formation; crystal structures of CyRPA alone and in complex with an antibody Fab fragment identify the PfRH5-interacting region of CyRPA (a functionally conserved epitope). X-ray crystallography; binding assay (CyRPA-PfRH5 interaction); monoclonal antibody blocking assay; in vitro growth inhibition assay eLife High 28195530
2018 Cryo-EM structure of the Rh5-CyRPA-Ripr complex at subnanometre resolution shows CyRPA is a critical mediator of complex assembly; blades 4–6 of the CyRPA β-propeller are contact sites for both Rh5 and Ripr; the limited contacts between Rh5-CyRPA and CyRPA-Ripr are consistent with dissociation of Rh5 and Ripr from CyRPA during membrane insertion; the full Rh5-CyRPA-Ripr complex binds the erythrocyte cell line JK-1 significantly better than Rh5 alone, and this enhanced binding involves insertion of Rh5 and Ripr into host membranes. Cryo-electron microscopy structure determination; erythrocyte binding assay; comparison with crystal structure of Rh5-basigin Nature High 30542156
2019 Antibodies specific for CyRPA prevent trimeric complex (Rh5/Ripr/CyRPA) formation, establishing that the inhibitory mechanism of anti-CyRPA antibodies acts at the level of complex assembly. Antibody blocking assay of complex formation; in vitro growth inhibition assay Cellular microbiology Medium 30965383
2019 In P. knowlesi, CyRPA (PkCyRPA) is essential for successful erythrocyte invasion in vitro, but unlike in P. falciparum, PkCyRPA does not form a complex with PkRIPR or with an RH5-like molecule; PkCyRPA appears to function independently of other parasite binding partners in P. knowlesi. Conditional knockdown (loss-of-function) in P. knowlesi; co-immunoprecipitation (negative result for PkCyRPA-PkRIPR complex) PLoS pathogens Medium 31185066
2022 CyRPA (as part of the PCRCR pentameric complex with PfPTRAMP, PfCSS, PfRH5, and PfRipr) is essential for erythrocyte invasion; the PCRCR complex functions to anchor contact between merozoite and erythrocyte membranes during strong parasite deformations; CyRPA is a component of this pentameric complex. Conditional knockout of PfPTRAMP and PfCSS; invasion-inhibitory nanobodies; lattice light-sheet microscopy; complex biochemistry Nature microbiology Medium 36396942
2023 The aspartic protease plasmepsin X (PMX) processes the PCRCR complex in micronemes by removing the N-terminal prodomain of PfRH5, which activates PCRCR function and unmasks the complex to bind basigin on the erythrocyte membrane; CyRPA is a component of this complex that is regulated by PMX processing. Conditional knockdown of PMX; biochemical processing assay; erythrocyte binding assay Nature communications Medium 37072430
2023 Cryo-EM structure of the PfRCR complex (PfRH5, PfCyRPA, PfRIPR) shows that PfCyRPA presents PfRH5 and forms part of the structured core; the elongated tail of PfRIPR is flexibly linked to the PfCyRPA-PfRH5 core; CyRPA-binding antibodies neutralize invasion through a steric mechanism (shown by modelling and erythrocyte-binding assay); a rigid, disulfide-locked PfRH5 can mediate efficient erythrocyte invasion (contradicting membrane-opening hypothesis). Cryo-electron microscopy structure determination; erythrocyte-binding assay; structural modelling Nature High 38123677
2022 Growth-inhibitory antibodies against CyRPA bind epitopes on a single face of CyRPA; pairs of non-competing inhibitory antibodies show strongly synergistic growth-inhibitory activity by forming lateral heterotypic interactions that slow antibody dissociation from CyRPA. Structural studies (antibody-CyRPA complexes); surface plasmon resonance (antibody dissociation kinetics); in vitro growth inhibition assay with antibody combinations Nature communications High 35177602
2024 CyRPA functions as a lectin that binds glycans terminating with α2-6-linked N-acetylneuraminic acid (Neu5Ac) on the erythrocyte surface; CyRPA has a >50-fold binding preference for human α2-6-linked Neu5Ac over non-human α2-6-linked N-glycolylneuraminic acid; lectin-binding sites were identified by molecular modelling and validated by mutagenesis; transgenic parasites expressing CyRPA with single amino acid exchange mutants in the lectin sites showed impaired invasion, demonstrating the functional importance of lectin activity. Glycan-binding assay; molecular modelling; site-directed mutagenesis; transgenic parasite lines with endogenous CyRPA point mutants; in vitro growth inhibition with small molecules and lectin-site-specific antibodies Cell reports High 38573856
2023 Anti-CyRPA monoclonal antibodies block invasion and additionally inactivate extracellular merozoites by triggering a developmental pathway normally seen only after successful invasion; combining anti-CyRPA and anti-PfRH5 mAbs enhances the degree of invasion inhibition observed by live-cell imaging. Live-cell imaging with monoclonal antibodies; in vitro growth inhibition assay PLoS pathogens Medium 37713419
2026 Structure-guided design of a CyRPA epitope mimic (PfCyRPA-EM) comprising blades 1 and 2 of the six-bladed β-propeller (the face exposed in the PCRCR complex and containing the epitopes of the most potent growth-inhibitory antibodies) elicits antibodies with superior growth-inhibitory activity at lower concentrations than full-length CyRPA in a preclinical model, establishing that blades 1 and 2 harbour the critical protective epitopes. Structure-guided protein engineering; immunization in preclinical model; in vitro growth inhibition assay EMBO molecular medicine Medium 41772083
2025 Sites 154 and 209 of PfCyRPA — previously reported as sufficient to switch glycan-binding preference between human (Neu5Ac) and ape glycans — are identical in P. falciparum and its gorilla precursor P. praefalciparum, and no other differences were found near the CyRPA glycan-binding sites; thus the gorilla precursor appears pre-adapted to bind human sialoglycans, and these two sites do not explain P. falciparum adaptation to humans. Comparative genome sequence analysis of P. falciparum, P. praefalciparum, and P. reichenowi Genome biology and evolution Low 39865504

Source papers

Stage 0 corpus · 65 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2018 Engineering a Rugged Nanoscaffold To Enhance Plug-and-Display Vaccination. ACS nano 248 30028591
2016 Essential Role of the PfRh5/PfRipr/CyRPA Complex during Plasmodium falciparum Invasion of Erythrocytes. Cell host & microbe 163 27374406
2015 Multiprotein complex between the GPI-anchored CyRPA with PfRH5 and PfRipr is crucial for Plasmodium falciparum erythrocyte invasion. Proceedings of the National Academy of Sciences of the United States of America 144 25583518
2018 Structure of Plasmodium falciparum Rh5-CyRPA-Ripr invasion complex. Nature 84 30542156
2017 Identification of highly-protective combinations of Plasmodium vivax recombinant proteins for vaccine development. eLife 65 28949293
2012 Passive immunoprotection of Plasmodium falciparum-infected mice designates the CyRPA as candidate malaria vaccine antigen. Journal of immunology (Baltimore, Md. : 1950) 63 22593616
2017 P113 is a merozoite surface protein that binds the N terminus of Plasmodium falciparum RH5. Nature communications 59 28186186
2017 Structure of the malaria vaccine candidate antigen CyRPA and its complex with a parasite invasion inhibitory antibody. eLife 59 28195038
2022 PCRCR complex is essential for invasion of human erythrocytes by Plasmodium falciparum. Nature microbiology 58 36396942
2020 The RH5-CyRPA-Ripr Complex as a Malaria Vaccine Target. Trends in parasitology 55 32359873
2017 Structural basis for inhibition of erythrocyte invasion by antibodies to Plasmodium falciparum protein CyRPA. eLife 53 28195530
2019 Neutralising antibodies block the function of Rh5/Ripr/CyRPA complex during invasion of Plasmodium falciparum into human erythrocytes. Cellular microbiology 47 30965383
2022 Heterotypic interactions drive antibody synergy against a malaria vaccine candidate. Nature communications 42 35177602
2019 Divergent roles for the RH5 complex components, CyRPA and RIPR in human-infective malaria parasites. PLoS pathogens 40 31185066
2019 Functional Comparison of Blood-Stage Plasmodium falciparum Malaria Vaccine Candidate Antigens. Frontiers in immunology 38 31214195
2018 Kinetics of antibody responses to PfRH5-complex antigens in Ghanaian children with Plasmodium falciparum malaria. PloS one 33 29883485
2023 The PfRCR complex bridges malaria parasite and erythrocyte during invasion. Nature 32 38123677
2024 Development of an improved blood-stage malaria vaccine targeting the essential RH5-CyRPA-RIPR invasion complex. Nature communications 27 38849365
2020 Bliss' and Loewe's additive and synergistic effects in Plasmodium falciparum growth inhibition by AMA1-RON2L, RH5, RIPR and CyRPA antibody combinations. Scientific reports 27 32678144
2020 Antibodies against a short region of PfRipr inhibit Plasmodium falciparum merozoite invasion and PfRipr interaction with Rh5 and SEMA7A. Scientific reports 26 32313230
2021 The Plasmodium falciparum Rh5 invasion protein complex reveals an excess of rare variant mutations. Malaria journal 21 34162366
2018 Identifying Immune Correlates of Protection Against Plasmodium falciparum Through a Novel Approach to Account for Heterogeneity in Malaria Exposure. Clinical infectious diseases : an official publication of the Infectious Diseases Society of America 19 29401272
2023 Plasmepsin X activates the PCRCR complex of Plasmodium falciparum by processing PfRh5 for erythrocyte invasion. Nature communications 17 37072430
2020 Vaccination with virosomally formulated recombinant CyRPA elicits protective antibodies against Plasmodium falciparum parasites in preclinical in vitro and in vivo models. NPJ vaccines 16 32025340
2020 Acquisition and decay of IgM and IgG responses to merozoite antigens after Plasmodium falciparum malaria in Ghanaian children. PloS one 16 33332459
2016 Generation of Plasmodium falciparum parasite-inhibitory antibodies by immunization with recombinantly-expressed CyRPA. Malaria journal 16 26979066
2021 Strain-Dependent Inhibition of Erythrocyte Invasion by Monoclonal Antibodies Against Plasmodium falciparum CyRPA. Frontiers in immunology 15 34447381
2022 RH5.1-CyRPA-Ripr antigen combination vaccine shows little improvement over RH5.1 in a preclinical setting. Frontiers in cellular and infection microbiology 14 36605129
2024 The essential malaria protein PfCyRPA targets glycans to invade erythrocytes. Cell reports 12 38573856
2023 Limited genetic variations of the Rh5-CyRPA-Ripr invasion complex in Plasmodium falciparum parasite population in selected malaria-endemic regions, Kenya. Frontiers in tropical diseases 12 38406638
2021 Plasmodium falciparum Cysteine-Rich Protective Antigen (CyRPA) Elicits Detectable Levels of Invasion-Inhibitory Antibodies during Natural Infection in Humans. Infection and immunity 10 34694918
2021 Identification and Immune Assessment of T Cell Epitopes in Five Plasmodium falciparum Blood Stage Antigens to Facilitate Vaccine Candidate Selection and Optimization. Frontiers in immunology 9 34305923
2022 Enhancing neutralization of Plasmodium falciparum using a novel monoclonal antibody against the rhoptry-associated membrane antigen. Scientific reports 8 35197516
2022 Scalable Process for High-Yield Production of PfCyRPA Using Insect Cells for Inclusion in a Malaria Virosome-Based Vaccine Candidate. Frontiers in bioengineering and biotechnology 8 35669054
2021 Antibody Combinations Targeting the Essential Antigens CyRPA, RH5, and MSP-119 Potently Neutralize Plasmodium falciparum Clinical Isolates From India and Africa. The Journal of infectious diseases 8 32989463
2020 The Structure of the Cysteine-Rich Domain of Plasmodium falciparum P113 Identifies the Location of the RH5 Binding Site. mBio 8 32900802
2023 The malaria blood stage antigen PfCyRPA formulated with the TLR-4 agonist adjuvant GLA-SE elicits parasite growth inhibitory antibodies in experimental animals. Malaria journal 6 37454145
2021 Genetic Diversity of Plasmodium vivax Cysteine-Rich Protective Antigen (PvCyRPA) in Field Isolates from Five Different Areas of the Brazilian Amazon. Genes 6 34828264
2020 Plasmodium vivax Cysteine-Rich Protective Antigen Polymorphism at Exon-1 Shows Recombination and Signatures of Balancing Selection. Genes 6 33379267
2023 Plasmodium sporozoites require the protein B9 to invade hepatocytes. iScience 5 36761022
2023 Construction, Expression, and Evaluation of the Naturally Acquired Humoral Immune Response against Plasmodium vivax RMC-1, a Multistage Chimeric Protein. International journal of molecular sciences 5 37511330
2023 The dual action of human antibodies specific to Plasmodium falciparum PfRH5 and PfCyRPA: Blocking invasion and inactivating extracellular merozoites. PLoS pathogens 5 37713419
2022 Expanding the Malaria Antibody Toolkit: Development and Characterisation of Plasmodium falciparum RH5, CyRPA, and CSP Recombinant Human Monoclonal Antibodies. Frontiers in cellular and infection microbiology 5 35782147
2022 Process development and preclinical evaluation of a major Plasmodium falciparum blood stage vaccine candidate, Cysteine-Rich Protective Antigen (CyRPA). Frontiers in immunology 5 36211427
2024 Dynamics of IgM and IgG Antibody Response Profile against Linear B-Cell Epitopes from Exoerythrocytic (CelTOS and TRAP) and Erythrocytic (CyRPA) Phases of Plasmodium vivax: Follow-Up Study. Antibodies (Basel, Switzerland) 3 39189240
2024 Leveraging Immunofocusing and Virus-like Particle Display to Enhance Antibody Responses to the Malaria Blood-Stage Invasion Complex Antigen PfCyRPA. Vaccines 3 39203985
2024 Characterization of T and B cell epitopes in PvCyRPA by studying the naturally acquired immune response in Brazilian Amazon communities. Scientific reports 3 39521783
2026 Extreme Genetic Diversity and Signatures of Balancing Selection in Plasmodium vivax Blood-Stage Antigens. The Journal of infectious diseases 2 41128014
2026 PTRAMP, CSS and Ripr form a conserved complex required for merozoite invasion of Plasmodium species into erythrocytes. Nature communications 2 41587959
2026 Identification of a growth-inhibitory epitope in PfRipr5, a malaria vaccine candidate against Plasmodium falciparum. Frontiers in immunology 2 41676142
2025 Plasmodium falciparum CyRPA Glycan Binding Does Not Explain Adaptation to Humans. Genome biology and evolution 2 39865504
2025 PTRAMP, CSS and Ripr form a conserved complex required for merozoite invasion of Plasmodium species into erythrocytes. bioRxiv : the preprint server for biology 2 40196582
2024 Immunogenicity of PvCyRPA, PvCelTOS and Pvs25 chimeric recombinant protein of Plasmodium vivax in murine model. Frontiers in immunology 2 38962015
2026 Genetic diversity in the Plasmodium falciparum next-generation blood stage vaccine candidate antigen PfCyRPA in Senegal. Scientific reports 1 41549078
2024 Genetic diversity in the Plasmodium falciparum next-generation blood stage vaccine candidate antigen PfCyRPA in Senegal. medRxiv : the preprint server for health sciences 1 39484257
2026 Structure-guided design of a PfCyRPA-based vaccine against blood-stage malaria. EMBO molecular medicine 0 41772083
2026 Analysis of monoclonal antibodies against the malaria invasion complex protein RIPR reveals the structural basis for synergistic antibody protection. Immunity 0 42285102
2025 The crystal structure of an uncharacterized domain of P113 from Plasmodium falciparum. Acta crystallographica. Section D, Structural biology 0 40192714
2025 PTRAMP, CSS and Ripr form a conserved complex required for merozoite invasion of Plasmodium species into erythrocytes. Research square 0 40343341
2025 Plasmodium vivax cysteine-rich protective antigen (PvCyRPA), an important element for vaccine strategies targeting P. vivax, interacts with human erythrocyte surface. Acta tropica 0 41205844
2025 Genetic diversity, natural selection, and immunological features of the Plasmodium vivax CyRPA protein: Implications for vaccine development. Gene 0 41238047
2025 Evaluating the potential of cross-species neutralization of anti-PfCyRPA and anti-PfRIPR Monoclonal Antibodies. bioRxiv : the preprint server for biology 0 41332710
2024 A targetable receptor-binding site on PfCyRPA to aid in the fight against malaria. Trends in parasitology 0 38604871
2023 A complex equation - adding to Plasmodium falciparum invasion. Trends in parasitology 0 36682939
2023 Reticulocyte Binding Protein Homologue 5 is a target of balancing selection in the Plasmodium falciparum population of Papua New Guinea. Frontiers in parasitology 0 39816834