Affinage · Plasmodium

RH4

PF3D7_0424200 · reticulocyte binding protein homologue 4

Annotated
2026-09-07
43 papers in source corpus 20 papers cited in narrative 21 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

RH4 (PF3D7_0424200) is a Plasmodium falciparum merozoite adhesin that mediates sialic acid-independent erythrocyte invasion and is the molecular determinant that lets parasites switch between invasion pathways: disruption of the gene abolishes switching to the sialic acid-independent route, and its transcriptional upregulation accompanies acquisition of that phenotype (PMID:16123303, PMID:16289357, PMID:29636510). RH4 binds the erythrocyte surface via a neuraminidase-resistant, protease-sensitive receptor identified as complement receptor 1 (CR1), engaging directly with a Kd of ~2.9 μM (PMID:19307208, PMID:20855594); the interaction maps to the membrane-distal complement control protein modules CCP1–3 of CR1, is centered on CCP1, and generates a ternary complex with C4b while inhibiting CR1's convertase decay-accelerating activity (PMID:21685372, PMID:24214979). Expression of RH4 is controlled epigenetically: silencing correlates with H3K9 trimethylation across its 5'-UTR, whereas repositioning of the locus to a perinuclear activation domain, increased promoter accessibility, and histone acetylation at the transcription start site activate the gene and drive the invasion-pathway switch, as demonstrated by targeted dCas9-based epigenetic editing (PMID:20080673, PMID:23245319, PMID:30584102). Beyond receptor binding, RH4 transmits an invasion signal through its cytoplasmic tail, which is phosphorylated in vitro and whose critical residues are required for erythrocyte penetration rather than attachment (PMID:26694741); the same cytoplasmic domain binds aldolase in competition with MTRAP, coupling the adhesin to the invasion machinery (PMID:27607074). RH4 is proteolytically cleaved by the rhomboid protease PfROM4 through recognition of its transmembrane domain and is shed as a 160-kDa fragment around the time of invasion, localizing to the tight junction (PMID:17040128, PMID:19307208, PMID:19614665). Anti-RH4 antibodies, monoclonal antibodies, nanobodies, and engineered soluble CR1 fragments that block the RH4-CR1 interaction inhibit invasion, establishing the interface as a vaccine and inhibitor target (PMID:21685372, PMID:26324715, PMID:42384414).

Mechanistic history

Synthesis pass · year-by-year structured walk · 13 steps
  1. 2005 High

    Established that RH4 is functionally required for parasites to switch from sialic acid-dependent to sialic acid-independent invasion, defining its role in invasion-pathway plasticity.

    Evidence Gene knockout with neuraminidase-treated erythrocyte invasion assays plus expression profiling, and microarray/RT-PCR/protein comparison of Dd2 versus Dd2/NM clones

    PMID:16123303 PMID:16289357

    Open questions at the time
    • Did not identify the erythrocyte receptor engaged in the sialic acid-independent pathway
    • Transactivating factors driving upregulation were implicated but not identified
  2. 2006 Medium

    Showed how RH4 is removed from the merozoite surface, identifying the rhomboid protease PfROM4 as cleaving RH4 through recognition of its transmembrane domain.

    Evidence Heterologous rhomboid cleavage assay with transmembrane domain-swap validation

    PMID:17040128

    Open questions at the time
    • Heterologous system, not demonstrated in native invasion
    • Timing and functional consequence of cleavage for invasion not established here
  3. 2007 Medium

    Localized the erythrocyte-binding activity to a conserved 30-kDa region of RH4 that binds neuraminidase-treated erythrocytes and competes with native protein, defining the functional adhesin domain.

    Evidence Recombinant fragment binding, competition and invasion inhibition assays; parallel antibody inhibition test

    PMID:17971435

    Open questions at the time
    • Antibodies to the binding fragment blocked binding but not invasion, indicating limited surface accessibility during invasion
    • Receptor identity still unknown at this stage
  4. 2009 Medium

    Characterized RH4 shedding and receptor properties and placed RH4 at the invasion tight junction, connecting binding to the physical act of invasion.

    Evidence Western blot of supernatants, enzyme-treatment binding assays, invasion inhibition with purified IgG, and immunolocalization of invasion intermediates

    PMID:19307208 PMID:19614665

    Open questions at the time
    • Molecular identity of the trypsin/chymotrypsin-sensitive receptor not yet resolved
    • Single-lab localization
  5. 2010 High

    Identified complement receptor 1 (CR1) as the direct erythrocyte receptor for RH4, resolving the long-standing question of the sialic acid-independent receptor.

    Evidence SPR affinity measurement (Kd 2.9 μM), binding to CR1-depleted erythrocytes, and competitive invasion inhibition with soluble CR1

    PMID:20855594

    Open questions at the time
    • Precise binding subdomain on CR1 not yet mapped
    • Structural basis of the interaction not defined
  6. 2010 High

    Defined the chromatin basis of RH4 regulation, linking H3K9 trimethylation-based silencing and nucleosome dynamics at the TSS to the transcriptional switch, and revealed compensatory transcriptional coupling with the EBL family.

    Evidence ChIP for histone marks and nucleosome occupancy across cell cycle in Dd2 vs Dd2NM; eba gene knockouts with PfRh transcriptional profiling; systematic HABP peptide binding and invasion inhibition

    PMID:20000683 PMID:20080673 PMID:21149582

    Open questions at the time
    • Factors that read/write the marks not identified
    • Mechanism linking EBL loss to RH4 upregulation not defined
  7. 2011 High

    Mapped the RH4 binding site to CR1 CCP modules 1–3 and showed the interaction inhibits complement convertase decay-acceleration, adding an immune-modulatory dimension to the invasion interaction.

    Evidence Recombinant CR1 fragment binding, competition invasion inhibition, functional complement assay, and ternary complex co-immunoprecipitation

    PMID:21685372

    Open questions at the time
    • Biological significance of convertase inhibition during invasion not established
    • Fine residue-level contacts not yet defined
  8. 2012 High

    Demonstrated that nuclear repositioning of the RH4 locus to a perinuclear activation domain precedes promoter accessibility and controls switching frequency, defining the spatial layer of RH4 regulation.

    Evidence Prokaryotic DNA methylase accessibility assay, FISH nuclear positioning, and transgenic forced activation of a proximal gene

    PMID:23245319

    Open questions at the time
    • Trans factors mediating repositioning not identified
    • Causal order between repositioning and epigenetic marks not fully resolved
  9. 2013 High

    Achieved structural and residue-level definition of the RH4-CR1 interface, fine-mapping to CCP1 and enabling engineered high-affinity binding sites, providing a template for inhibitor design.

    Evidence Homologous substitution mutagenesis of CR1, engineered CCP8 binding site, SPR affinity, and NMR + SAXS solution structure of CCP1–3; heparin affinity chromatography localizing RH4 to apical organelles

    PMID:24212193 PMID:24214979

    Open questions at the time
    • No co-complex structure of RH4 bound to CR1
    • Heparin binding of RH4 not functionally validated (Low confidence)
  10. 2015 High

    Established that RH4 actively transmits an invasion signal through its cytoplasmic tail rather than serving only as an adhesin, distinguishing attachment from penetration.

    Evidence In vitro phosphorylation assay, site-directed mutagenesis of the cytoplasmic tail, and live-cell imaging of transgenic parasites; parallel blocking-mAb and engineered soluble CR1 inhibitor characterization

    PMID:26324715 PMID:26694741

    Open questions at the time
    • Kinase(s) acting on the tail in vivo not defined
    • Downstream signaling effectors of the phosphorylated residues unknown
  11. 2016 Medium

    Connected the RH4 cytoplasmic tail to the invasion motor by showing it binds aldolase in competition with MTRAP, with phosphorylation modulating affinity.

    Evidence Direct and competition binding assays with the cytoplasmic tail and aldolase, plus in vitro phosphorylation with CDPK1 and PKA

    PMID:27607074

    Open questions at the time
    • In vivo relevance of the aldolase interaction not demonstrated for RH4 specifically
    • Functional link between tail phosphorylation and motor coupling not tested in parasites
  12. 2018 High

    Provided causal proof that histone acetylation at the RH4 TSS is sufficient to activate the gene and switch invasion pathways, and that environmental culture conditions can drive the switch via RH4-CR1.

    Evidence CRISPR/dCas9-epigenetic effector targeting of the RH4 TSS with invasion phenotyping; suspension-culture switching with anti-CR1 inhibition

    PMID:29636510 PMID:30584102

    Open questions at the time
    • Endogenous signals triggering acetylation not identified
    • Physiological trigger of environmental switching in vivo unknown
  13. 2026 Medium

    Advanced RH4 as an intervention target by generating invasion-blocking nanobodies and computationally stabilized RH4 scaffolds retaining CR1 and antibody binding.

    Evidence Nanobody generation, affinity and invasion inhibition assays, and computational protein design with functional validation

    PMID:42384414

    Open questions at the time
    • In vivo protective efficacy not shown
    • Strain-transcendent breadth of the inhibitors not established

Open questions

Synthesis pass · forward-looking unresolved questions
  • How the RH4 cytoplasmic tail phosphorylation signal is decoded to convert attachment into penetration, and which trans factors execute the epigenetic/nuclear switch, remain unresolved.
  • In vivo kinase(s) and downstream effectors of the cytoplasmic tail signal unknown
  • Identity of the chromatin/repositioning trans factors controlling RH4 switching unknown
  • No experimental RH4-CR1 co-complex structure

Mechanism profile

Synthesis pass · controlled-vocabulary classification
Partners
ALDOLASEC4B (IN TERNARY COMPLEX WITH CR1)CR1 (COMPLEMENT RECEPTOR 1, ERYTHROCYTE RECEPTOR, CCP1-3/CCP1)MTRAP (COMPETES FOR ALDOLASE BINDING)PFROM4 (PFE0340C RHOMBOID PROTEASE)
Complex memberships
RH4 cytoplasmic tail-aldolase complexRH4-CR1 (CCP1-3) receptor-adhesin complexTernary complex of RH4, CR1 CCP1-3, and C4b

Evidence

Reading pass · 21 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2005 RH4 expression correlates with sialic acid-independent invasion, and disruption of the RH4 gene abolishes the ability of P. falciparum parasites to switch from sialic acid-dependent to sialic acid-independent invasion pathways, establishing RH4 as essential for pathway switching. Gene disruption (knockout) with invasion phenotype assay using neuraminidase-treated erythrocytes; expression profiling Science (New York, N.Y.) High 16123303
2005 RH4 is transcriptionally upregulated in the Dd2/NM clone (sialic acid-independent) compared to Dd2 (sialic acid-dependent), and this upregulation is reflected at the protein level; the upregulation is not associated with DNA sequence changes in or around the gene, implicating transactivating factors. Oligonucleotide microarray expression profiling, real-time RT-PCR, protein expression analysis, DNA sequencing Molecular and biochemical parasitology Medium 16289357
2006 PfROM4 (PFE0340c), a Plasmodium falciparum rhomboid intramembrane protease, cleaves RH4 (as well as other adhesins) in a heterologous cleavage assay, relying on the RH4 transmembrane domain as the substrate recognition element. Heterologous enzymatic cleavage assay with rhomboid proteases; transmembrane domain swap experiments PLoS pathogens Medium 17040128
2007 Recombinant RH4 (rRH4(30), a 30-kDa conserved region fragment) binds strongly to neuraminidase-treated (sialic acid-depleted) erythrocytes, and this recombinant fragment competes with native RH4 for erythrocyte binding and blocks invasion of neuraminidase-treated erythrocytes by the Dd2/NM clone. Recombinant protein erythrocyte binding assay; competition binding assay; invasion inhibition assay Proceedings of the National Academy of Sciences of the United States of America Medium 17971435
2007 Although antibodies to rRH4(30) block native RH4 binding to erythrocytes, these antibodies failed to block parasite invasion, suggesting RH4 is inaccessible to antibody-mediated inhibition during the invasion process. Invasion inhibition assay with anti-RH4 antibodies Proceedings of the National Academy of Sciences of the United States of America Medium 17971435
2009 RH4 is shed into culture supernatants as a 160-kDa proteolytic fragment and binds to the erythrocyte surface via a receptor that is neuraminidase-resistant but trypsin- and chymotrypsin-sensitive; antibodies against the RH4 binding domain block native RH4 erythrocyte binding and inhibit sialic acid-independent invasion. Western blot of culture supernatants; enzyme-treatment erythrocyte binding assay; invasion inhibition assay with purified IgG Infection and immunity Medium 19307208
2009 RH4 and RH1 undergo proteolytic cleavage events during merozoite invasion, with ectodomain processing producing fragments consistent with rhomboid protease cleavage within the transmembrane domain; the processed proteins are released into the supernatant around the time of invasion. RH4 (along with RH1 and EBA-175) localizes to the tight junction during invasion. Western blot analysis of invasion intermediates; supernatant fractionation; immunofluorescence/localization assays Cellular microbiology Medium 19614665
2010 Complement receptor 1 (CR1) is the erythrocyte receptor for RH4; RH4 and CR1 interact directly with a Kd of 2.9 μM. RH4 binding correlates with CR1 surface density, invasion via sialic acid-independent pathways is reduced in low-CR1 erythrocytes, and soluble CR1 competitively blocks RH4 binding and inhibits sialic acid-independent invasion. Direct binding assay (surface plasmon resonance for Kd); erythrocyte binding assay with CR1-depleted cells; competition invasion inhibition with soluble CR1 Proceedings of the National Academy of Sciences of the United States of America High 20855594
2010 Epigenetic silencing of RH4 in Dd2 (non-expressing clone) is associated with H3K9 trimethylation throughout the 5'-UTR of the RH4 gene throughout the cell cycle; activation of RH4 in Dd2NM correlates with reduced nucleosome occupancy at the +1 position downstream of the transcription start site and with histone modifications associated with active transcription at 44 h post-invasion. Chromatin immunoprecipitation (ChIP) for histone modifications (H3K9me3, active marks); nucleosome occupancy assay at the RH4 TSS Proceedings of the National Academy of Sciences of the United States of America High 20080673
2011 RH4 binds to complement control protein modules 1–3 (CCP1–3) at the membrane-distal N-terminus of CR1; RH4 did not bind significantly to other CR1 constructs (e.g. CCP15–17 which is 85% identical to CCP1–3). RH4 binding to CR1 specifically inhibited CR1's convertase decay-accelerating activity, and evidence for a ternary complex between CCP1–3, C4b, and RH4 was obtained. Recombinant CR1 fragment binding assay; competition invasion inhibition; functional complement assay; co-immunoprecipitation (ternary complex) Blood High 21685372
2010 Loss of EBL protein function results in upregulation of PfRh family transcription (including RH4), demonstrating functional cooperativity between EBL and PfRh families and compensatory transcriptional regulation. Single and double knockout of eba genes with transcriptional profiling of PfRh genes; growth inhibition assays Infection and immunity Medium 21149582
2012 Nuclear repositioning of the RH4 locus from a silent to a conserved perinuclear activation domain precedes promoter accessibility; promoter accessibility (measured by prokaryotic DNA methylase accessibility assay) is tightly correlated with active RH4 transcription. Forced activation of a proximal gene repositions the RH4 locus and increases RH4 activation frequency in a subpopulation of parasites. Prokaryotic DNA methylase accessibility assay; fluorescence in situ hybridization (FISH) for nuclear positioning; transgenic parasite lines Cell host & microbe High 23245319
2013 The PfRH4 binding site on CR1 was fine-mapped to CCP1 by homologous substitution mutagenesis; an artificial PfRH4-binding site engineered into CCP8 by substituting putative PfRH4-interacting residues from CCP1 had ~30-fold higher affinity for RH4 than the native CCP1 site. Solution structure of CCP1–3 was determined by NMR and small-angle X-ray scattering. ELISA, co-immunoprecipitation, surface plasmon resonance, homologous substitution mutagenesis of CR1, NMR + SAXS structural determination The Journal of biological chemistry High 24214979
2013 RH4 (along with other EBL and RH family members) binds to heparin; heparin-binding proteins of the RH and Duffy binding-like families localize preferentially to apical organelles. The interaction was identified by heparin affinity chromatography fractionation followed by immunoblot. Heparin affinity chromatography; immunoblot; immunofluorescence localization Scientific reports Low 24212193
2015 The cytoplasmic tail of RH4 is phosphorylated in vitro, and specific residues within the RH4 cytoplasmic domain are required for successful parasite invasion; transgenic parasites with mutations in the critical cytoplasmic domain residues attach to but fail to penetrate erythrocytes, as shown by live cell imaging. In vitro phosphorylation assay; site-directed mutagenesis of RH4 cytoplasmic tail; transgenic parasite live cell imaging PLoS pathogens High 26694741
2015 Anti-RH4 monoclonal antibodies that block the RH4-CR1 interaction inhibit RH4 binding to erythrocytes and abolish the RH4-CR1 invasion pathway; epitope mapping identified distinct functional regions within RH4 involved in CR1 interaction. Engineered CR1 protein fragments based on mutagenesis of the RH4 binding site on CR1 bind tightly to RH4 (by SPR) and function as soluble inhibitors of the RH4-CR1 invasion pathway. Anti-RH4 monoclonal antibody characterization; epitope mapping; surface plasmon resonance; invasion inhibition assay; CR1 mutagenesis The Journal of biological chemistry High 26324715
2010 Twenty conserved, largely alpha-helical high-activity binding peptides (HABPs) spanning the RH4 protein bind to 32, 25, 22, and 20 kDa erythrocyte membrane molecules in a chymotrypsin- and/or trypsin-sensitive manner (nanomolar Kd); anti-RH4 rabbit sera and RH4 HABPs inhibited merozoite invasion in vitro. Synthetic peptide erythrocyte binding assay (20-mer peptides spanning full RH4); receptor molecular weight determination by affinity interaction; invasion inhibition assay Journal of medicinal chemistry Medium 20000683
2016 The cytoplasmic tail (CTD) of RH4 binds to aldolase; MTRAP competes with RH4 for binding to aldolase, indicating overlapping binding sites. Phosphorylation of the CTDs of EBL and RH family proteins (including RH4) by kinases increases their affinity for aldolase in some cases. Direct binding assay (CTD-aldolase); competition binding assay; in vitro phosphorylation with CDPK1 and PKA PloS one Medium 27607074
2018 CRISPR/dCas9 fused to epigenetic effector domains specifically activated RH4 transcription by writing histone acetylation at the RH4 transcription start site region, leading to a switch from sialic acid-dependent to sialic acid-independent invasion pathways. CRISPR/dCas9-epigenetic effector domain fusion; histone acetylation writing at RH4 TSS; invasion pathway phenotyping Proceedings of the National Academy of Sciences of the United States of America High 30584102
2018 P. falciparum strains Dd2 and W2mef spontaneously switch to sialic acid-independent invasion phenotype when cultured with gentle shaking (suspension), accompanied by upregulation of RH4; returning cultures to static conditions reverses the switch. The increased SA-independent invasion in suspension culture was inhibited by anti-CR1 antibodies, confirming RH4-CR1 pathway involvement. Invasion phenotype assay (neuraminidase-treated erythrocytes); RT-PCR for RH4 expression; invasion inhibition with anti-CR1 antibodies; culture condition manipulation Scientific reports Medium 29636510
2026 Nanobodies raised against RH4 bind with high affinity across several epitopes, block RH4-CR1 receptor engagement, and inhibit parasite invasion of red blood cells. Computationally designed stabilized RH4 variants encompassing the conserved scaffold retained binding to monoclonal antibodies, nanobodies, and CR1. Nanobody generation and characterization; binding affinity measurement; invasion inhibition assay; computational protein design with functional validation The Biochemical journal Medium 42384414

Source papers

Stage 0 corpus · 43 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2005 Molecular mechanism for switching of P. falciparum invasion pathways into human erythrocytes. Science (New York, N.Y.) 226 16123303
2006 Two Plasmodium rhomboid proteases preferentially cleave different adhesins implicated in all invasive stages of malaria. PLoS pathogens 180 17040128
2010 Complement receptor 1 is the host erythrocyte receptor for Plasmodium falciparum PfRh4 invasion ligand. Proceedings of the National Academy of Sciences of the United States of America 174 20855594
2010 Reticulocyte and erythrocyte binding-like proteins function cooperatively in invasion of human erythrocytes by malaria parasites. Infection and immunity 117 21149582
2012 Enhancing blockade of Plasmodium falciparum erythrocyte invasion: assessing combinations of antibodies against PfRH5 and other merozoite antigens. PLoS pathogens 112 23144611
2007 Recombinant Plasmodium falciparum reticulocyte homology protein 4 binds to erythrocytes and blocks invasion. Proceedings of the National Academy of Sciences of the United States of America 75 17971435
2002 Gene structure and expression of a Plasmodium falciparum 220-kDa protein homologous to the Plasmodium vivax reticulocyte binding proteins. Molecular and biochemical parasitology 69 12034462
2005 Upregulation of expression of the reticulocyte homology gene 4 in the Plasmodium falciparum clone Dd2 is associated with a switch in the erythrocyte invasion pathway. Molecular and biochemical parasitology 63 16289357
2009 Antibodies to reticulocyte binding protein-like homologue 4 inhibit invasion of Plasmodium falciparum into human erythrocytes. Infection and immunity 58 19307208
2010 Epigenetic control of the variable expression of a Plasmodium falciparum receptor protein for erythrocyte invasion. Proceedings of the National Academy of Sciences of the United States of America 57 20080673
2018 Epigenetic editing by CRISPR/dCas9 in Plasmodium falciparum. Proceedings of the National Academy of Sciences of the United States of America 56 30584102
2006 Expression of Plasmodium falciparum genes involved in erythrocyte invasion varies among isolates cultured directly from patients. Molecular and biochemical parasitology 56 16837080
2009 Reticulocyte binding protein homologues are key adhesins during erythrocyte invasion by Plasmodium falciparum. Cellular microbiology 53 19614665
2016 The association between naturally acquired IgG subclass specific antibodies to the PfRH5 invasion complex and protection from Plasmodium falciparum malaria. Scientific reports 52 27604417
2012 The Plasmodium falciparum erythrocyte invasion ligand Pfrh4 as a target of functional and protective human antibodies against malaria. PloS one 50 23028883
2016 Identification of a reticulocyte-specific binding domain of Plasmodium vivax reticulocyte-binding protein 1 that is homologous to the PfRh4 erythrocyte-binding domain. Scientific reports 43 27244695
2015 Plasmodium falciparum Adhesins Play an Essential Role in Signalling and Activation of Invasion into Human Erythrocytes. PLoS pathogens 43 26694741
2011 Plasmodium falciparum uses a key functional site in complement receptor type-1 for invasion of human erythrocytes. Blood 43 21685372
2012 Identification of a potent combination of key Plasmodium falciparum merozoite antigens that elicit strain-transcending parasite-neutralizing antibodies. Infection and immunity 41 23184525
2015 Variation in Plasmodium falciparum erythrocyte invasion phenotypes and merozoite ligand gene expression across different populations in areas of malaria endemicity. Infection and immunity 37 25870227
2019 RTS,S/AS01E immunization increases antibody responses to vaccine-unrelated Plasmodium falciparum antigens associated with protection against clinical malaria in African children: a case-control study. BMC medicine 32 31409398
2013 Analyses of interactions between heparin and the apical surface proteins of Plasmodium falciparum. Scientific reports 32 24212193
2012 Anti-Plasmodium falciparum invasion ligand antibodies in a low malaria transmission region, Loreto, Peru. Malaria journal 32 23110555
2012 Plasmodium falciparum field isolates from South America use an atypical red blood cell invasion pathway associated with invasion ligand polymorphisms. PloS one 26 23118907
2018 Plasmodium falciparum strains spontaneously switch invasion phenotype in suspension culture. Scientific reports 25 29636510
2013 Using mutagenesis and structural biology to map the binding site for the Plasmodium falciparum merozoite protein PfRh4 on the human immune adherence receptor. The Journal of biological chemistry 24 24214979
2012 Nuclear repositioning precedes promoter accessibility and is linked to the switching frequency of a Plasmodium falciparum invasion gene. Cell host & microbe 24 23245319
2011 Differences in erythrocyte receptor specificity of different parts of the Plasmodium falciparum reticulocyte binding protein homologue 2a. Infection and immunity 23 21628513
2024 Complement receptor 1 is the human erythrocyte receptor for Plasmodium vivax erythrocyte binding protein. Proceedings of the National Academy of Sciences of the United States of America 22 38261617
2013 Acquired antibodies to merozoite antigens in children from Uganda with uncomplicated or severe Plasmodium falciparum malaria. Clinical and vaccine immunology : CVI 13 23740926
2021 HIV infection and placental malaria reduce maternal transfer of multiple antimalarial antibodies in Mozambican women. The Journal of infection 12 33636218
2017 Acquisition, maintenance and adaptation of invasion inhibitory antibodies against Plasmodium falciparum invasion ligands involved in immune evasion. PloS one 12 28787025
2015 Characterization of Inhibitors and Monoclonal Antibodies That Modulate the Interaction between Plasmodium falciparum Adhesin PfRh4 with Its Erythrocyte Receptor Complement Receptor 1. The Journal of biological chemistry 10 26324715
2019 Antibody Reactivity to Merozoite Antigens in Ghanaian Adults Correlates With Growth Inhibitory Activity Against Plasmodium falciparum in Culture. Open forum infectious diseases 9 31294045
2019 Few Plasmodium falciparum merozoite ligand and erythrocyte receptor pairs show evidence of balancing selection. Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases 7 30735814
2016 The Binding of Plasmodium falciparum Adhesins and Erythrocyte Invasion Proteins to Aldolase Is Enhanced by Phosphorylation. PloS one 7 27607074
2010 Well-defined regions of the Plasmodium falciparum reticulocyte binding protein homologue 4 mediate interaction with red blood cell membrane. Journal of medicinal chemistry 7 20000683
2023 Effects of anti-malarial prophylaxes on maternal transfer of Immunoglobulin-G (IgG) and association to immunity against Plasmodium falciparum infections among children in a Ugandan birth cohort. PloS one 3 36812236
2020 Population genetic and biophysical evidences reveal that purifying selection shapes the genetic landscape of Plasmodium falciparum RH ligands in Chhattisgarh and West Bengal, India. Malaria journal 3 33054833
2009 Case-control approach to identify Plasmodium falciparum polymorphisms associated with severe malaria. PloS one 2 19421327
2023 Recent increase in low complexity polygenomic infections and sialic acid-independent invasion pathways in Plasmodium falciparum from Western Gambia. Parasites & vectors 1 37653544
2022 Phenotypic characterization of Ghanaian P. falciparum clinical isolates reveals a homogenous parasite population. Frontiers in immunology 1 36211335
2026 Nanobodies against Plasmodium adhesins that block receptor engagement and malaria parasite invasion. The Biochemical journal 0 42384414