Affinage · Plasmodium

Showing PF3D7_0905400 — RHOPH3 is a alias.

RhopH3

PF3D7_0905400 · high molecular weight rhoptry protein 3

Annotated
2026-09-08
41 papers in source corpus 21 papers cited in narrative 21 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

RhopH3 (PF3D7_0905400) is an essential rhoptry protein of P. falciparum that is indispensable both for erythrocyte invasion and for establishing the nutrient-uptake channel of the infected red cell (PMID:1775161, PMID:28252384, PMID:28221136). It assembles non-covalently with CLAG3 and RhopH2 into the high molecular weight RhopH complex (PMID:7517517, PMID:33393463), and cryo-EM of the native soluble complex resolves its architecture at atomic resolution: RhopH3 forms a large binding interface with CLAG3 while making minimal direct contact with RhopH2, and contributes to the extensive intramolecular disulfide bonding that shields CLAG3's putative transmembrane helix within the complex core (PMID:33393463, PMID:34446549). RhopH3 is required for correct rhoptry targeting and trafficking of the entire complex, and its conditional knockdown both reduces invasion and abolishes new-permeability-pathway/PSAC activity in parasites that do invade; unlike clag3, rhoph3 cannot be deleted, marking it as uniquely essential for channel function (PMID:28252384, PMID:28221136, PMID:32069335). During invasion RhopH3 and RhopH2 are discharged into the nascent parasitophorous vacuole rather than directly into the host cytoplasm, and only after export into the erythrocyte does the CLAG3/RhopH2/RhopH3 channel assemble and activate nutrient uptake, a compartmentalization that prevents premature channel formation (PMID:35393572). RhopH3 also engages host determinants directly, binding erythrocyte band 3 (5ABC region) as part of a ternary complex with MSP1(19) in the sialic-acid-independent invasion pathway (PMID:25157665) and using surface Cyclophilin B as a receptor (PMID:29146974). Its function is gated by phosphorylation at serine 804, which controls rhoptry localization and discharge and is critical for invasion, with PfCDPK1 identified as the candidate kinase (PMID:33024030), while its translation timing is repressed post-transcriptionally by the RNA-binding protein PfAlba1 until schizogony (PMID:26415947).

Mechanistic history

Synthesis pass · year-by-year structured walk · 19 steps
  1. 1991 Medium

    Establishing that RhopH3 is a defined rhoptry protein created the molecular entity on which all subsequent invasion and channel work would build.

    Evidence cDNA/genomic cloning with Western blotting and immunoelectron microscopy in P. falciparum merozoites

    PMID:1775161

    Open questions at the time
    • No function assigned at identification
    • Relationship to other rhoptry proteins not yet defined
  2. 1993 Medium

    Tracking RhopH3 through rhoptry biogenesis showed its expression and trafficking are stage-coordinated with organelle maturation, framing it as a regulated rhoptry cargo.

    Evidence Subcellular fractionation, sucrose gradients, immunoelectron microscopy and Northern blotting across nuclear division stages

    PMID:8433718

    Open questions at the time
    • Trafficking signals not identified
    • Mechanism coordinating mRNA and protein timing unknown at this stage
  3. 1994 Medium

    Immunoprecipitation resolved whether RhopH3 acts alone or in a complex, defining it as a non-covalent member of the high molecular weight rhoptry complex.

    Evidence Immunoprecipitation with a panel of monoclonal antibodies plus immunofluorescence/immuno-EM

    PMID:7517517

    Open questions at the time
    • Stoichiometry and binding interfaces undefined
    • Functional consequence of complex membership unknown
  4. 1997 Medium

    Epitope mapping distinguished a 110 kDa precursor from a 105 kDa product, establishing that RhopH3 undergoes C-terminal proteolytic processing.

    Evidence Overlapping peptide scanning and isoform-specific antisera by Western blotting

    PMID:9106189

    Open questions at the time
    • Protease responsible not identified
    • Functional role of processing not determined
  5. 2003 Low

    Co-localization with RAMA implicated the Golgi-vesicle pathway in delivering RhopH3 to rhoptries, addressing how the protein reaches its organelle.

    Evidence Immunofluorescence, brefeldin A inhibition and immuno-EM in P. falciparum

    PMID:14613941

    Open questions at the time
    • Co-localization inference without direct RhopH3 pull-down
    • Direct RAMA-RhopH3 interaction not demonstrated
    • Single lab
  6. 2008 Medium

    Peptide-binding and invasion-inhibition experiments provided the first evidence that RhopH3 engages the erythrocyte surface during invasion.

    Evidence Synthetic peptide erythrocyte-binding assays with enzyme-treated cells and invasion inhibition in P. falciparum

    PMID:18593818

    Open questions at the time
    • Erythrocyte receptor not identified at this stage
    • Peptide binding may not reflect native protein geometry
  7. 2008 Medium

    Following the RhopH complex after invasion revealed transfer beyond the parasite into the erythrocyte cytoplasm, foreshadowing a host-cell role for RhopH3.

    Evidence Immunofluorescence and subcellular fractionation of infected erythrocytes

    PMID:18508137

    Open questions at the time
    • Export mechanism undefined
    • Functional consequence in host cytoplasm not yet linked to nutrient transport
  8. 2010 Medium

    Reciprocal pull-downs placed RhopH3 in a broader merozoite invasion assembly and showed anti-RhopH3 antibodies block invasion, functionally implicating it in RBC entry.

    Evidence Co-immunoprecipitation with tandem MS and invasion inhibition from merozoite lysates

    PMID:21175202

    Open questions at the time
    • Direct versus indirect associations not resolved
    • Which interactions are functionally required unclear
  9. 2014 Medium

    Identifying band 3 as a direct RhopH3 ligand gave a molecular receptor for its sialic-acid-independent invasion role.

    Evidence Yeast two-hybrid, co-IP, ternary complex reconstitution and recombinant-protein invasion inhibition

    PMID:25157665

    Open questions at the time
    • Binding region on RhopH3 not mapped to atomic detail
    • Relative contribution versus other receptors unquantified
  10. 2015 Medium

    RIP-seq and translational profiling explained how RhopH3 protein appears only at the right stage, identifying PfAlba1-mediated translational repression.

    Evidence RNA immunoprecipitation-seq, ribosome occupancy and mRNA level analysis with tagged overexpression

    PMID:26415947

    Open questions at the time
    • Signal releasing the mRNA in schizonts unknown
    • Direct PfAlba1 binding site on RhopH3 mRNA not mapped
  11. 2017 High

    Conditional knockdown and failed knockout established RhopH3 as essential, required for complex assembly/trafficking, invasion, and PSAC-mediated nutrient uptake.

    Evidence DiCre conditional knockdown, knockout attempts, invasion assays, sorbitol/nutrient uptake and trafficking readouts across two independent labs

    PMID:28221136 PMID:28252384

    Open questions at the time
    • Separating invasion role from channel role at the molecular level incomplete
    • Whether RhopH3 forms channel pore directly unknown
  12. 2017 Medium

    Co-IP tied RhopH3 to RhopH2, RhopH1, host cytoskeleton and exported remodeling proteins, and metabolic assays linked complex integrity to nutrient/cofactor uptake and pyrimidine synthesis.

    Evidence Co-immunoprecipitation with conditional RhopH2 knockdown, metabolomics and growth assays

    PMID:28252383

    Open questions at the time
    • Metabolic phenotype driven via RhopH2 knockdown rather than RhopH3 directly
    • Direct cytoskeleton contacts of RhopH3 not resolved
  13. 2017 Medium

    Identifying erythrocyte-surface Cyclophilin B as a RhopH3 receptor added a second host determinant and placed RhopH3 in a receptor complex with Basigin and PfRh5.

    Evidence Localization/binding studies, co-IP and invasion inhibition with Cyclosporin A and peptide CDP3

    PMID:29146974

    Open questions at the time
    • Direct versus complex-mediated RhopH3-Cyclophilin B binding not fully separated
    • No reconstitution of the receptor complex
  14. 2020 High

    Phosphomutant analysis showed S804 phosphorylation gates RhopH3 rhoptry localization and discharge and is critical for invasion, naming PfCDPK1 as candidate kinase.

    Evidence CRISPR-Cas9 S804A mutant, invasion assays, immunofluorescence localization and kinase candidate identification in P. falciparum 3D7

    PMID:33024030

    Open questions at the time
    • Direct PfCDPK1 phosphorylation of RhopH3 not biochemically proven
    • How phosphorylation mechanistically controls discharge unresolved
  15. 2020 High

    Comparing rhoph3 with clag3 showed only RhopH3 is strictly required for nutrient uptake, defining its unique essentiality for PSAC/NPP activity.

    Evidence Knockout attempts, sorbitol/nutrient uptake assays and genetic cross linkage analysis

    PMID:32069335

    Open questions at the time
    • Molecular basis of RhopH3's non-redundant role in the channel undefined
    • Whether RhopH3 contributes to conductive pathway itself unknown
  16. 2021 High

    Cryo-EM structures of the native soluble complex resolved RhopH3's architecture, showing it interfaces largely with CLAG3, minimally with RhopH2, and helps shield CLAG3's transmembrane helix via disulfide bonding.

    Evidence Single-particle cryo-EM at 2.9 A with MS stoichiometry and cryoID, two independent structural studies

    PMID:33393463 PMID:34446549

    Open questions at the time
    • Membrane-inserted channel conformation not captured
    • Trigger for the conformational change to membrane insertion unresolved
  17. 2021 Medium

    Reciprocal IP defined exported and cytoskeletal/Maurer's cleft partners of the RhopH3 complex, but their knockdown left NPP activity intact, distinguishing associated proteins from channel-essential ones.

    Evidence Reciprocal co-IP, conditional knockdown, sorbitol/NPP uptake assay and MS proteomics in P. falciparum 3D7

    PMID:33774908

    Open questions at the time
    • Functional role of the exported partners undefined
    • Direct binding to RhopH3 versus other complex members not resolved
  18. 2022 High

    Live-cell tracking showed RhopH3 is discharged into the parasitophorous vacuole and only assembles the channel after export, revealing spatial control that prevents premature channel formation.

    Evidence Live-cell and super-resolution imaging, immunofluorescence, conditional knockdown and nutrient uptake assays in P. falciparum 3D7

    PMID:35393572

    Open questions at the time
    • Export machinery requirements for RhopH3 not fully defined here
    • Signal timing assembly relative to phosphorylation not integrated
  19. 2026 Medium

    Testing the P. vivax homologue extended RhopH3 erythrocyte-binding function across species, mapping binding to specific recombinant regions.

    Evidence Recombinant region expression with immunoprecipitation and rosette-formation binding assays in P. vivax

    PMID:42314857

    Open questions at the time
    • Host receptor for PvRhopH3 not identified
    • Functional invasion role in P. vivax not tested

Open questions

Synthesis pass · forward-looking unresolved questions
  • It remains unresolved whether RhopH3 contributes structurally to the conductive PSAC pore itself or acts solely as an assembly/trafficking-essential subunit, and how S804 phosphorylation and disulfide-gated conformational change mechanistically drive discharge and membrane insertion.
  • No membrane-inserted channel structure
  • Direct kinase-substrate proof for PfCDPK1-RhopH3 lacking
  • Molecular basis of RhopH3's unique non-redundancy versus CLAG3 unknown

Mechanism profile

Synthesis pass · controlled-vocabulary classification
Partners
CLAG3 (RHOPH1) [#2, #12, #16, #17]EXPORTED PROTEIN PF3D7_1401200 AND CYTOSKELETAL/MAURER'S CLEFT PARTNERS [#18]HUMAN CYCLOPHILIN B [#13]HUMAN ERYTHROCYTE BAND 3 (5ABC REGION) [#9]MSP1(19) [#9]PFALBA1 (RHOPH3 MRNA BINDING) [#8]PFCDPK1 (CANDIDATE KINASE) [#14]RAMA (CO-LOCALIZATION) [#4]RHOPH2 [#2, #12, #16, #17, #19]
Complex memberships
Host receptor complex: Cyclophilin B, Basigin, RhopH3, PfRh5 [#13]Merozoite invasion assembly with MSP-1(42), RhopH1, RAP-1, RAP-2, MSP-3/6/7/9 [#7]RhopH complex (CLAG3 : RhopH2 : RhopH3, 1:1:1) [#16, #17]Ternary complex RhopH3-MSP1(19)-band 3 5ABC [#9]

Evidence

Reading pass · 21 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1991 RhopH3 (PF3D7_0905400) was identified as a 105 kDa protein located in the rhoptries of P. falciparum merozoites, encoded by a genomic sequence with 7 exons including 2 mini-exons, lacking tandem repeats, and containing B cell epitopes that induce antibody responses during natural infection. cDNA/genomic cloning, Western blotting, immunoelectron microscopy Molecular and biochemical parasitology Medium 1775161
1993 During rhoptry biogenesis in P. falciparum, RhopH3 (as Rhop-H3) is first detectable in small granular low-density vesicle compartments (~1.12 g/ml sucrose) at the four-nucleus stage together with RhopH2, then later appears in higher-density mature rhoptries (~1.16 g/ml) at the 16-nucleus stage; RhopH3 mRNA peaks at the 8-nucleus stage, demonstrating stage-specific expression coordinated with rhoptry biogenesis. Subcellular fractionation, sucrose gradient centrifugation, immunoelectron microscopy, Northern blotting Molecular and biochemical parasitology Medium 8433718
1994 Monoclonal antibodies recognizing the RhopH complex immunoprecipitated RhopH3 together with RhopH1 and RhopH2, confirming RhopH3 is a non-covalently associated component of the high molecular weight rhoptry complex; some mAbs recognized RhopH3 alone while others co-precipitated RhopH3 with RhopH1 or RhopH2, indicating distinct epitope accessibility. Immunoprecipitation, immunofluorescence, immunoelectron microscopy Parasitology Medium 7517517
1997 Two major monoclonal antibody binding sites on RhopH3 were mapped to amino acids 823–828 (TDNTY/TDNTYK) and ~residue 850 of the C-terminal region. Antibodies to the ~850 site reacted exclusively with the 110 kDa form of RhopH3 but not the 105 kDa form, providing evidence that the 105 kDa RhopH3 polypeptide is generated from the 110 kDa form by C-terminal proteolytic processing. Overlapping peptide scanning, systematic amino acid replacement, Western blotting with isoform-specific antisera Molecular and biochemical parasitology Medium 9106189
2003 RhopH3 and RAP1 were found in close apposition with RAMA in early vesicles/pre-rhoptries, suggesting direct protein-protein interactions; this co-localization was disrupted by brefeldin A, implicating RAMA in trafficking RhopH3 into rhoptries via the Golgi-vesicle pathway. Immunofluorescence microscopy, brefeldin A inhibition, immunoelectron microscopy The Journal of biological chemistry Low 14613941
2008 After red blood cell invasion by P. falciparum, the merozoite-acquired RhopH complex (including RhopH3) is transferred not only to the parasitophorous vacuole membrane but also to defined domains of the red blood cell cytoplasm, with possible transient association with Maurer's clefts. Immunofluorescence microscopy, subcellular fractionation of infected erythrocytes Molecular and biochemical parasitology Medium 18508137
2008 Fourteen synthetic peptides derived from RhopH3 (PF3D7_0905400) bound to human erythrocytes with saturable kinetics and nanomolar dissociation constants; binding was partially sensitive to sialic acid removal and glycoprotein-disrupting enzyme treatments. These peptides inhibited P. falciparum merozoite invasion of erythrocytes by up to 90% at 200 µM. Synthetic peptide erythrocyte binding assays, enzyme-treated erythrocytes, cross-linking assays, circular dichroism, invasion inhibition assays Protein science Medium 18593818
2010 Proteomic pull-down experiments with anti-PfMSP-1 and anti-PfRhopH3 antibodies from merozoite lysates identified a complex containing PfRhopH3, PfMSP-1(42), PfRhopH1, PfRAP-1, PfRAP-2, MSP-3, MSP-6, MSP-7, and MSP-9, present at schizont/merozoite stages but not ring stage. Anti-PfRhopH3 antibodies blocked erythrocyte invasion. Co-immunoprecipitation / pull-down, tandem mass spectrometry, invasion inhibition assay Journal of proteome research Medium 21175202
2015 The RNA-binding protein PfAlba1 binds RhopH3 mRNA in trophozoites and represses its translation at this stage; release of the mRNA from PfAlba1 complex in mature schizonts correlates with protein synthesis, establishing post-transcriptional translational timing control of RhopH3 expression. RNA immunoprecipitation with deep sequencing, ribosome occupancy, mRNA steady-state level analysis, epitope-tagged overexpression Genome biology Medium 26415947
2014 A direct biochemical interaction between RhopH3 and human erythrocyte band 3 (specifically the 5ABC extracellular region) was established by yeast two-hybrid screen and confirmed biochemically. RhopH3 forms a ternary complex with MSP1(19) and band 3 5ABC, and a recombinant segment of RhopH3 inhibited P. falciparum invasion of erythrocytes, implicating this interaction in the sialic acid-independent invasion pathway. Yeast two-hybrid, co-immunoprecipitation, recombinant protein invasion inhibition assay, anti-peptide antibody inhibition assay Biochimica et biophysica acta Medium 25157665
2017 Conditional knockdown of RhopH3 in P. falciparum substantially reduces erythrocyte invasion capacity. Parasites that do invade despite RhopH3 knockdown show defective nutrient import (new permeability pathway / PSAC activity) and die. Knockdown of RhopH3 also disrupts the entire RhopH complex, interfering with organellar targeting and subsequent trafficking of all complex members. Conditional knockdown (DiCre-based truncation), invasion assays, sorbitol/nutrient uptake assays, immunofluorescence, Western blotting eLife High 28252384
2017 Conditional knockdown of RhopH3 in P. falciparum disrupts the entire RhopH complex assembly, interfering with organellar (rhoptry) targeting; knockdown abolishes nutrient channel (PSAC) activity; rhoph3 gene knockout was not viable, confirming RhopH3 is essential. RhopH3 contributes to erythrocyte invasion either through ligand-receptor interactions or subsequent parasite internalization steps. Conditional knockdown, gene knockout attempt, nutrient uptake assays, protein trafficking assays eLife High 28221136
2017 RhopH3 interacts with RhopH2, RhopH1, the erythrocyte cytoskeleton, and exported proteins involved in host cell remodeling, as shown by co-immunoprecipitation in the context of investigating the RhopH complex. Knockdown of RhopH2 (which depletes the RhopH2–RhopH3 interaction) leads to reduced nutrient and cofactor uptake and decreased pyrimidine synthesis. Co-immunoprecipitation, conditional knockdown of RhopH2, metabolomics, growth assays eLife Medium 28252383
2017 Human Cyclophilin B (present on erythrocyte surface) acts as a receptor for RhopH3 (PF3D7_0905400) during merozoite invasion. RhopH3 binds to red blood cells, and Cyclosporin A treatment (blocking Cyclophilin B) prevents merozoite invasion. A multi-protein complex involving Cyclophilin B, Basigin, RhopH3, and PfRh5 was identified. Localization and binding studies, co-immunoprecipitation, invasion inhibition with Cyclosporin A and peptide CDP3 Nature communications Medium 29146974
2020 RhopH3 is phosphorylated at serine 804 (S804) in P. falciparum parasites. CRISPR-Cas9 mutation of S804 to alanine (phosphomutant R3_S804A) demonstrated that this phosphorylation is critical for RBC invasion but not intraerythrocytic development. S804 phosphorylation regulates RhopH3 localization to rhoptries and its discharge from the parasite. PfCDPK1 was identified as a candidate kinase responsible for RhopH3-S804 phosphorylation, and it regulates RhopH3 secretion. CRISPR-Cas9 phosphomutant generation, invasion assays, immunofluorescence localization, kinase candidate identification mBio High 33024030
2020 rhoph3 cannot be disrupted (knockout not viable) in P. falciparum because nutrient uptake is abolished in its absence, in contrast to clag3 which can be knocked out without abolishing transport under standard conditions. This establishes RhopH3 as uniquely essential for PSAC/NPP activity. Gene knockout attempts, sorbitol/nutrient uptake assays, genetic cross linkage analysis PLoS pathogens High 32069335
2021 Cryo-EM structure of the native soluble RhopH trafficking complex at 2.9 Å resolution reveals RhopH3 forms large binding interfaces with CLAG3.1 but makes minimal direct contact with RhopH2. The complex assembles with 1:1:1 stoichiometry (CLAG3:RhopH2:RhopH3). RhopH3 contributes to stabilization via extensive disulfide bonding (contributing to 13 intramolecular disulfide bonds across the complex). Predicted transmembrane helices of CLAG3 are shielded within the soluble complex core. Single-particle cryo-EM (2.9 Å), mass spectrometry, cryoID structural determination of endogenous complex eLife High 33393463
2021 Cryo-EM structure of the native RhopH complex shows CLAG3.1 is positioned centrally between RhopH2 and RhopH3, with RhopH3 sharing a substantial binding interface with CLAG3.1. RhopH3 stabilization involves intramolecular disulfide bonds; 13 disulfide bonds total stabilize the complex. The putative CLAG3 transmembrane helix (residues 1210–1223) is buried in a helical bundle, suggesting that membrane insertion requires a large conformational rearrangement, possibly triggered by allosteric disulfide bond breakage. Cryo-EM structure determination, mass spectrometry, cryoID program for subunit identification Proceedings of the National Academy of Sciences of the United States of America High 34446549
2021 Five exported proteins (including the most strongly associated PF3D7_1401200) interact with all members of the RhopH complex (CLAG3, RhopH2, RhopH3) as shown by reciprocal immunoprecipitation, but conditional knockdown of these proteins had no effect on NPP/sorbitol uptake activity. Additional protein complexes (cytoskeletal and Maurer's cleft/J-dot complexes) associated with RhopH3-containing complex were identified by MS proteomics. Reciprocal co-immunoprecipitation, conditional knockdown, sorbitol/NPP uptake assay, mass spectrometry proteomics Cellular microbiology Medium 33774908
2022 During merozoite invasion, RhopH3 and RhopH2 are released into the nascent parasitophorous vacuole (not directly into the host cell cytoplasm as CLAG3 is), and the full RhopH complex has not yet formed at this point. Export of RhopH2 and RhopH3 from the parasitophorous vacuole into the erythrocyte cytoplasm enables assembly of CLAG3/RhopH2/RhopH3 complexes and their incorporation into the host cell membrane, coinciding with activation of nutrient uptake. This compartmentalization prevents premature channel assembly. Live-cell imaging, immunofluorescence, conditional knockdown, nutrient uptake assays, super-resolution microscopy Communications biology High 35393572
2026 In P. vivax, the RhopH3 homologue (PvRhopH3) binds human erythrocytes; three expressed recombinant regions (R1, R2, R3) were tested and regions R1 and R3 showed erythrocyte binding capability by immunoprecipitation and rosette-formation assays, with R1 having the highest binding rates. Recombinant protein expression, immunoprecipitation, rosette-formation erythrocyte binding assay Acta tropica Medium 42314857

Source papers

Stage 0 corpus · 41 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2014 New antigens for a multicomponent blood-stage malaria vaccine. Science translational medicine 142 25080477
2003 Characterization of a membrane-associated rhoptry protein of Plasmodium falciparum. The Journal of biological chemistry 106 14613941
2017 Plasmodium falciparum parasites deploy RhopH2 into the host erythrocyte to obtain nutrients, grow and replicate. eLife 92 28252383
2017 An essential dual-function complex mediates erythrocyte invasion and channel-mediated nutrient uptake in malaria parasites. eLife 90 28221136
2017 The Plasmodium falciparum rhoptry protein RhopH3 plays essential roles in host cell invasion and nutrient uptake. eLife 79 28252384
2001 The high molecular mass rhoptry protein, RhopH1, is encoded by members of the clag multigene family in Plasmodium falciparum and Plasmodium yoelii. Molecular and biochemical parasitology 72 11738712
2005 Apical expression of three RhopH1/Clag proteins as components of the Plasmodium falciparum RhopH complex. Molecular and biochemical parasitology 68 15953647
1991 Primary structure of a Plasmodium falciparum rhoptry antigen. Molecular and biochemical parasitology 68 1775161
2008 The RhopH complex is transferred to the host cell cytoplasm following red blood cell invasion by Plasmodium falciparum. Molecular and biochemical parasitology 57 18508137
2015 The PfAlba1 RNA-binding protein is an important regulator of translational timing in Plasmodium falciparum blood stages. Genome biology 50 26415947
1987 A cDNA clone expressing a rhoptry protein of Plasmodium falciparum. Molecular and biochemical parasitology 47 2823136
2011 Functional analysis of epigenetic regulation of tandem RhopH1/clag genes reveals a role in Plasmodium falciparum growth. Molecular microbiology 46 21320181
2007 Diversity and evolution of the rhoph1/clag multigene family of Plasmodium falciparum. Molecular and biochemical parasitology 46 18155305
2021 Malaria parasites use a soluble RhopH complex for erythrocyte invasion and an integral form for nutrient uptake. eLife 44 33393463
2003 Characterisation of the rhoph2 gene of Plasmodium falciparum and Plasmodium yoelii. Molecular and biochemical parasitology 41 12615335
1993 Biogenesis of rhoptry organelles in Plasmodium falciparum. Molecular and biochemical parasitology 40 8433718
2020 Complex nutrient channel phenotypes despite Mendelian inheritance in a Plasmodium falciparum genetic cross. PLoS pathogens 33 32069335
2010 Proteome analysis reveals a large merozoite surface protein-1 associated complex on the Plasmodium falciparum merozoite surface. Journal of proteome research 31 21175202
2023 Anti-merozoite antibodies induce natural killer cell effector function and are associated with immunity against malaria. Science translational medicine 30 36753561
1994 Analysis of the high molecular weight rhoptry complex of Plasmodium falciparum using monoclonal antibodies. Parasitology 29 7517517
2014 Human erythrocyte band 3 functions as a receptor for the sialic acid-independent invasion of Plasmodium falciparum. Role of the RhopH3-MSP1 complex. Biochimica et biophysica acta 28 25157665
2021 Native structure of the RhopH complex, a key determinant of malaria parasite nutrient acquisition. Proceedings of the National Academy of Sciences of the United States of America 26 34446549
1994 Immunogenicity and antigenicity of a Plasmodium falciparum protein fraction (90-110 kDa) able to protect squirrel monkeys against asexual blood stages. Vaccine 26 8303938
2021 Characterisation of complexes formed by parasite proteins exported into the host cell compartment of Plasmodium falciparum infected red blood cells. Cellular microbiology 23 33774908
2006 The Plasmodium falciparum RhopH2 promoter and first 24 amino acids are sufficient to target proteins to the rhoptries. Parasitology international 22 17175193
2020 Live-Cell FRET Reveals that Malaria Nutrient Channel Proteins CLAG3 and RhopH2 Remain Associated throughout Their Tortuous Trafficking. mBio 19 32900800
2007 Identifying and characterising the Plasmodium falciparum RhopH3 Plasmodium vivax homologue. Biochemical and biophysical research communications 19 17511961
2020 Phosphorylation of Rhoptry Protein RhopH3 Is Critical for Host Cell Invasion by the Malaria Parasite. mBio 18 33024030
2022 RhopH2 and RhopH3 export enables assembly of the RhopH complex on P. falciparum-infected erythrocyte membranes. Communications biology 17 35393572
2017 Human Cyclophilin B forms part of a multi-protein complex during erythrocyte invasion by Plasmodium falciparum. Nature communications 16 29146974
2001 Conserved regions of the Plasmodium yoelii rhoptry protein RhopH3 revealed by comparison with the P. falciparum homologue. Molecular and biochemical parasitology 16 11223137
2008 Identification of Plasmodium falciparum RhopH3 protein peptides that specifically bind to erythrocytes and inhibit merozoite invasion. Protein science : a publication of the Protein Society 15 18593818
1997 Characterisation of the binding sites of monoclonal antibodies reacting with the Plasmodium falciparum rhoptry protein RhopH3. Molecular and biochemical parasitology 15 9106189
2021 Identification of a Novel RAMA/RON3 Rhoptry Protein Complex in Plasmodium falciparum Merozoites. Frontiers in cellular and infection microbiology 8 33537242
2020 Plasmodium falciparum Clag9-Associated PfRhopH Complex Is Involved in Merozoite Binding to Human Erythrocytes. Infection and immunity 8 31712270
2016 Malaria Parasite CLAG3, a Protein Linked to Nutrient Channels, Participates in High Molecular Weight Membrane-Associated Complexes in the Infected Erythrocyte. PloS one 4 27299521
2026 Evolutionary rate covariation across malaria parasite species enables inference of protein interactions. bioRxiv : the preprint server for biology 2 41659435
2026 Identification of serine/arginine-rich splicing factor 1-interacting proteins in Plasmodium berghei. Malaria journal 0 41634752
2026 A CRISPR-Based Mutagenesis Strategy for Examining CLAG3 Helix 44 Contribution to Malaria Parasite Nutrient Uptake Channels. Genes 0 42074580
2026 The Plasmodium vivax high molecular weight (HMW) rhoptry 3 protein (RhopH3) is involved in human red blood cell binding. Acta tropica 0 42314857
2026 Evolutionary Rate Covariation Across Malaria Parasite Species Enables Inference of Protein Interactions. Genome biology and evolution 0 42664386