Affinage · Plasmodium

SBP1

PBANKA_1101300 · skeleton-binding protein 1

Annotated
2026-09-07
35 papers in source corpus 23 papers cited in narrative 23 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

SBP1 (PBANKA_1101300/PfSBP1) is an integral membrane protein resident at the Maurer's clefts of malaria parasite-infected erythrocytes that is essential for the export machinery delivering parasite virulence antigens to the host red-cell surface (PMID:11087921, PMID:16520384). Genetic disruption of SBP1 in P. falciparum retains PfEMP1 within Maurer's clefts, abolishes its surface display and cytoadhesion, and is rescued by complementation, establishing SBP1 as an indispensable component of the PfEMP1 translocation pathway acting during cleft formation at the parasitophorous vacuole membrane (PMID:16520384, PMID:17023587); loss of SBP1 correspondingly collapses antibody recognition and opsonic phagocytosis of infected cells, placing it upstream of the dominant surface antigens targeted by acquired immunity (PMID:27193441). SBP1 anchors Maurer's clefts to the erythrocyte membrane skeleton through its C-terminal cytoplasmic domain, which binds a 35 kDa skeletal protein and, more specifically, sub-domains of protein 4.1R and spectrin, an interaction necessary but not sufficient for PfEMP1 surface delivery, while an essential lumenal role for its N-terminal domain remains uncharacterized (PMID:11087921, PMID:25883090). SBP1 reaches the clefts via a distinctive PEXEL/VTS-independent, Plasmepsin V-independent route: its internal hydrophobic segment serves as an internal signal for secretory-pathway entry and transits an ER-lumenal intermediate, with N-terminal negatively charged domains governing membrane orientation and export competence (PMID:19054387, PMID:23387285, PMID:37000891). This trafficking is chaperone-dependent, engaging PfBiP and the group II chaperonin PfTRiC during early soluble export intermediates and passing through electron-dense cytoplasmic material and the parasitophorous vacuolar space before cleft delivery (PMID:18691247, PMID:25615740, PMID:31669509). SBP1 function is deeply conserved: cross-species complementation with P. falciparum SBP1 restores CD36 binding, sequestration and virulence in P. berghei SBP1 knockouts, and in a P. berghei model SBP1-mediated sequestration inhibits spontaneous resolution of malaria-associated acute respiratory distress syndrome rather than driving initial pathology (PMID:27225796, PMID:34843584).

Mechanistic history

Synthesis pass · year-by-year structured walk · 13 steps
  1. 2000 Medium

    Establishing that SBP1 is a Maurer's cleft integral membrane protein whose cytoplasmic C-terminus engages the host skeleton framed it as a candidate linker between parasite-induced structures and the erythrocyte membrane.

    Evidence Immunoprecipitation and biochemical characterization plus cross-species antibody labelling of infected erythrocytes

    PMID:11087921

    Open questions at the time
    • Identity of the 35 kDa erythrocyte partner not determined
    • Functional consequence of the anchoring interaction not tested
  2. 2005 Medium

    Identifying host LANCL1 as a partner of the SBP1 C-terminal cytoplasmic domain extended the anchoring model to specific host cytosolic recruitment at the cleft surface.

    Evidence Co-immunoprecipitation with mass spectrometry identification and immunofluorescence in infected erythrocytes

    PMID:15811525

    Open questions at the time
    • Proposed role in preventing premature RBC rupture not directly tested
    • Single lab, no functional loss-of-function of the interaction
  3. 2006 High

    Gene disruption resolved whether SBP1 is merely a structural resident or functionally required, showing it is essential for translocating PfEMP1 to the infected-cell surface and for cytoadhesion, and placing its action at the PVM during cleft formation.

    Evidence Targeted knockout with genetic complementation, immunofluorescence, and adhesion/antibody-reactivity assays in P. falciparum

    PMID:16520384 PMID:17023587

    Open questions at the time
    • Molecular mechanism of PfEMP1 hand-off not defined
    • Whether SBP1 acts directly on PfEMP1 or indirectly via cleft architecture unresolved
  4. 2006 Medium

    Linking a cleft-resident PP1 to the phosphorylation state of the SBP1 N-terminal domain connected reversible SBP1 modification to red-cell membrane stability and merozoite release.

    Evidence Co-immunoprecipitation and calyculin A inhibition with observation of blocked merozoite release

    PMID:16548885

    Open questions at the time
    • Phosphorylation sites not mapped at residue resolution
    • Direct causal link between SBP1 phosphorylation and release not isolated from other PP1 substrates
  5. 2008 Medium

    Dissecting the export signals showed SBP1 uses a PEXEL-independent route in which its transmembrane segment acts as an internal signal and negatively charged N-terminal domains license export, defining the sequence logic of a PEXEL-negative exported protein.

    Evidence Domain-deletion and chimeric reporter mutagenesis with fractionation and microscopy; domain swaps onto REX2; CAD conditional export system identifying PfBiP interaction

    PMID:18691247 PMID:19054387 PMID:19170882

    Open questions at the time
    • Machinery recognizing the internal signal not identified
    • Order of chaperone engagement not fully resolved
  6. 2013 Medium

    An in vitro cleavage assay confirmed SBP1 export is independent of Plasmepsin V processing, cementing its classification within the PEXEL-negative export pathway.

    Evidence In vitro Plasmepsin V cleavage assay with N-terminal sequencing

    PMID:23387285

    Open questions at the time
    • Negative in vitro result; alternative processing events not excluded
  7. 2015 Medium

    Mapping SBP1 binding to protein 4.1R/spectrin sub-domains and to the chaperonin PfTRiC clarified both the host-skeleton anchoring interface and a soluble chaperone-assisted export intermediate, while revealing that skeleton binding is necessary but not sufficient for PfEMP1 surface delivery.

    Evidence GST pulldowns and domain mapping with recombinant skeleton proteins; co-IP and fractionation identifying PfTRiC interaction mapped to the N-terminal domain

    PMID:25615740 PMID:25883090

    Open questions at the time
    • The additional essential lumenal N-terminal function remains unidentified
    • Interactions not validated by orthogonal in-cell methods
  8. 2016 High

    Cross-species knockout and complementation established that SBP1 function is evolutionarily conserved, mediating CD36 binding, sequestration and virulence in P. berghei, and that its trafficking pathway underlies immune recognition of infected cells.

    Evidence P. berghei knockout with P. falciparum complementation and in vivo sequestration/virulence readouts; P. falciparum deletion coupled to antibody-binding and opsonic phagocytosis assays; PkSBP1 localization by IFA and immuno-EM

    PMID:27193441 PMID:27225796 PMID:27732628

    Open questions at the time
    • Conserved molecular partners across species not fully mapped
    • How SBP1 loss translates to loss of specific surface antigens beyond PfEMP1 not delineated
  9. 2017 Medium

    Demonstrating that SBP1 can bind PHISTc protein PFD1140w and PfEMP1 simultaneously identified it as a scaffolding node in a tripartite complex, suggesting how it organizes PfEMP1 within clefts.

    Evidence In vitro binding with recombinant proteins, co-IP, and co-localization

    PMID:29155505

    Open questions at the time
    • Tripartite complex shown in vitro; physiological stoichiometry and in-cell assembly not established
  10. 2019 Medium

    Temporal proximity biotinylation, AP-MS interactome mapping, and ultrastructural localization resolved SBP1's export itinerary and its distinct pre- and post-export interactor sets, including a candidate translocon-domain protein and an intermediate through electron-dense material and the PV space.

    Evidence TurboID proximity proteomics with conditional mutants; AP-MS interactome; immunoelectron microscopy

    PMID:31476617 PMID:31669509 PMID:37772444

    Open questions at the time
    • Direct extraction/translocon mechanism at the parasite plasma membrane not proven
    • Most interactome hits not individually validated
  11. 2021 Medium

    An epistasis experiment in an MA-ARDS model showed SBP1-mediated sequestration inhibits spontaneous disease resolution rather than being required for initial lung pathology, refining SBP1's role in disease progression.

    Evidence SBP1 knockout P. berghei NK65 mouse model with bioluminescence imaging, cytokine RT-qPCR, CD8+ T-cell flow cytometry, and histopathology

    PMID:34843584

    Open questions at the time
    • Mechanism linking sequestration to sustained inflammation not defined
    • Single lab, single strain
  12. 2023 Medium

    Topology analysis revealed a productive ER-lumenal intermediate for SBP1 export, showing its internal hydrophobic sequence does not span the ER membrane and refining the mechanism of secretory-pathway entry.

    Evidence Chimeric reporters with KDEL retention, intact-cell topology assays, microscopy and mass spectrometry

    PMID:37000891

    Open questions at the time
    • How the lumenal intermediate is converted to a membrane-integral cleft form not resolved
    • Single lab
  13. 2024 Medium

    Extending SBP1 study to gametocytes showed it localizes to cleft-like structures there and associates with PfHSP70-1 and PfHSP70-x, indicating chaperone-assisted handling across life-cycle stages.

    Evidence Co-immunoprecipitation with mass spectrometry and immunofluorescence in gametocyte-infected erythrocytes

    PMID:38331312

    Open questions at the time
    • Functional role of SBP1 in gametocytes not tested
    • Chaperone interactions not functionally dissected

Open questions

Synthesis pass · forward-looking unresolved questions
  • The essential lumenal N-terminal function of SBP1, the direct molecular mechanism by which it hands PfEMP1 to the surface, and the identity of the machinery recognizing its internal export signal remain unresolved.
  • No structure of SBP1 or its complexes
  • Mechanism of PfEMP1 translocation downstream of skeleton anchoring unknown
  • Translocon that extracts SBP1 for export not definitively identified

Mechanism profile

Synthesis pass · controlled-vocabulary classification
Partners
35 KDA ERYTHROCYTE SKELETAL PROTEIN [#0]CBP2 CYTOPLASMIC DOMAIN [#21]ERYTHROCYTE PROTEIN 4.1R [#9]ERYTHROCYTE SPECTRIN [#9]HOST LANCL1 [#4]PFBIP [#7]PFEMP1 (FUNCTIONAL/COMPLEX PARTNER) [#1, #14, #20]PFHSP70-1 [#19]PFHSP70-X [#19]PFJ23 [#20]PFTRIC (GROUP II CHAPERONIN) [#10]PHISTC PFD1140W [#14]
Complex memberships
SBP1–PHISTc(PFD1140w)–PfEMP1 tripartite complex [#14]SBP1–PfJ23–PfEMP1 tripartite complex [#20]

Evidence

Reading pass · 23 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2000 SBP1 (PfSBP1) is an integral membrane protein of Maurer's clefts in P. falciparum-infected erythrocytes; its carboxy-terminal domain, exposed in the host cell cytoplasm, interacts with a 35 kDa erythrocyte skeletal protein, suggesting it participates in anchoring Maurer's clefts to the erythrocyte submembrane skeleton. Antibodies to both termini of PfSBP1 also labelled vesicular structures in P. berghei-infected erythrocytes, indicating conservation across malaria species. Immunoprecipitation with hyperimmune sera, biochemical characterization, antibody labelling of infected erythrocytes from multiple Plasmodium species Molecular and biochemical parasitology Medium 11087921
2006 Targeted gene disruption of SBP1 in P. falciparum prevented PfEMP1 surface expression on infected red blood cells and abolished cytoadhesion; PfEMP1 was retained in Maurer's clefts and Maurer's clefts were displaced from the erythrocyte periphery. Complementation with sbp1 restored PfEMP1 surface expression and adhesion, demonstrating SBP1 is essential for PfEMP1 translocation to the infected erythrocyte surface. Targeted gene disruption (knockout), genetic complementation, immunofluorescence, adhesion assays The Journal of cell biology High 16520384
2006 PfSBP1 functions at the parasitophorous vacuole membrane (PVM) to load PfEMP1 into Maurer's clefts during formation of these structures; loss of PfSBP1 abolished PfEMP1 surface display and the major antibody reactivity of multigravid women directed at PfEMP1. Genetic disruption of SBP1, immunofluorescence microscopy, antibody reactivity assays with immune sera Blood High 17023587
2006 Parasite protein phosphatase 1 (PP1), localized to Maurer's clefts, modulates the phosphorylation status of the amino-terminal domain of PfSBP1 within the lumen of Maurer's clefts, as shown by co-immunoprecipitation and phosphatase inhibition. Hyperphosphorylation of PfSBP1 induced by the PP1 inhibitor calyculin A in late schizonts prevented merozoite release, linking SBP1 phosphorylation state to red blood cell membrane stability. Co-immunoprecipitation, pharmacological inhibition with calyculin A, observation of merozoite release block Cellular microbiology Medium 16548885
2005 The carboxy-terminal cytoplasmic domain of PfSBP1 on Maurer's clefts interacts with the host erythrocyte cytosolic protein LANCL1; LANCL1 is specifically recruited to the surface of Maurer's clefts in mature P. falciparum blood stages, implicating this interaction in preventing premature rupture of the red blood cell membrane. Co-immunoprecipitation, mass spectrometry identification of LANCL1, immunofluorescence localization in infected erythrocytes Molecular and biochemical parasitology Medium 15811525
2008 The transmembrane domain of PfSBP1 functions as an internal signal sequence for entry into the parasite's secretory pathway and transport to the parasite plasma membrane; trafficking beyond the parasite plasma membrane additionally requires N-terminal domains with high negative net charge, which influence protein solubility, membrane orientation, and subcellular localization. PfSBP1 lacks the PEXEL/VTS motif and is not N-terminally processed. Domain-deletion mutagenesis, chimeric reporter constructs, biochemical fractionation, immunofluorescence Traffic (Copenhagen, Denmark) Medium 19054387
2008 The N-terminal region and transmembrane domain of PfSBP1 can functionally replace the corresponding regions in the PEXEL-negative exported protein REX2 to promote export, demonstrating these sequence features are shared among PEXEL-negative exported proteins and are functionally interchangeable. Chimeric protein domain-swap constructs expressed in P. falciparum, fluorescence microscopy Molecular microbiology Medium 19170882
2008 PfSBP1 physically interacts with the molecular chaperone PfBiP during early export steps, as revealed by the conditional aggregation domain (CAD) export system; this interaction occurs prior to arrival at Maurer's clefts. Conditional protein export system (CAD domain fused to full-length PfSBP1), co-immunoprecipitation of intermediate complexes Cellular microbiology Medium 18691247
2013 Plasmepsin V does not cleave the N-terminal sequence of SBP1 (a PEXEL-negative exported protein), establishing that SBP1 export is independent of Plasmepsin V processing. In vitro Plasmepsin V cleavage assay, N-terminal sequencing Traffic (Copenhagen, Denmark) Medium 23387285
2015 A defined region of PfSBP1 binds specifically to sub-domains of two major erythrocyte membrane skeleton components, protein 4.1R and spectrin; these interactions anchor Maurer's clefts to the red blood cell membrane skeleton but are necessary yet not sufficient for PfEMP1 translocation to the RBC surface. The N-terminal domain of SBP1 within the Maurer's cleft lumen plays an essential but unidentified additional role. GST pulldown, domain-deletion mapping, binding assays with recombinant erythrocyte skeleton proteins, co-localization Biochimica et biophysica acta Medium 25883090
2015 Three resident Maurer's cleft membrane proteins including PfSBP1 are exported as soluble forms in the red cell cytoplasm and associate with the parasite group II chaperonin PfTRiC; the domain of interaction with PfTRiC was mapped within the amino-terminal domain of PfSBP1. Co-immunoprecipitation, domain mapping, subcellular fractionation Traffic (Copenhagen, Denmark) Medium 25615740
2016 P. berghei orthologues of SBP1 and MAHRP1 were identified; red blood cells infected with P. berghei parasites lacking SBP1 fail to bind the endothelial receptor CD36 and show reduced sequestration and virulence in mice. Complementation of P. berghei SBP1 knockout parasites with P. falciparum SBP1 restored sequestration and virulence, demonstrating evolutionary conservation of SBP1 function across divergent malaria parasites. Gene knockout in P. berghei, cross-species complementation with P. falciparum SBP1, in vivo sequestration assays (bioluminescence imaging), CD36 binding assays, virulence assessment in mice Nature communications High 27225796
2016 Genetic deletion of SBP1 in P. falciparum dramatically reduced antibody recognition of infected erythrocytes and abolished the ability of human antibodies to promote opsonic phagocytosis, demonstrating that SBP1 is part of a critical trafficking pathway for the dominant surface antigens (primarily PfEMP1) targeted by acquired human immunity. Genetic deletion of SBP1, flow cytometry-based antibody binding assays, opsonic phagocytosis assays, multiple parasite isolates and immune sera from different populations Cellular and molecular life sciences : CMLS High 27193441
2016 P. knowlesi SBP1 (PkSBP1), when expressed as an epitope-tagged recombinant protein, localizes to membranous structures (Sinton and Mulligan stipplings) analogous to Maurer's clefts in monkey and human erythrocytes; when expressed in P. falciparum-infected erythrocytes, PkSBP1 co-localizes with PfSBP1 at Maurer's clefts, demonstrating conservation of the trafficking pathway. Transgenic parasite expression of epitope-tagged PkSBP1, immunofluorescence assay, immunoelectron microscopy, co-localization with PfSBP1 PloS one Medium 27732628
2017 PHISTc protein PFD1140w interacts with both PfSBP1 and PfEMP1 simultaneously in vitro, forming a tripartite complex; a direct binding interaction between recombinant PHIST proteins and PfSBP1 was detected, identifying PfSBP1 as a novel binding partner of PHISTc family members. In vitro pulldown/binding assays with recombinant proteins, co-immunoprecipitation, co-localization by immunofluorescence The FEBS journal Medium 29155505
2019 Using time-resolved proximity biotinylation (SBP1 fused to TurboID), two groups of SBP1 interactors were identified: early (pre-export) and late (post-export). Two membrane-associated proteins were identified as pre-export interactors, one with a predicted translocon domain, suggesting they facilitate extraction of SBP1 from the parasite plasma membrane for export. TurboID proximity biotinylation fused to SBP1, label-free quantitative proteomics, conditional mutants of candidate proteins, fluorescence localization Journal of cell science Medium 37772444
2019 A comprehensive SBP1 interactome was determined in P. falciparum-infected erythrocytes using unbiased proteomic approaches; SBP1 interactomes revealed numerous exported proteins and potential interactors associated with SBP1 intracellular trafficking, including host-parasite protein interactions. The exported protein MAL8P1.4 was linked to P. falciparum virulence via this interaction network. Proteomic interaction mapping (co-immunoprecipitation/AP-MS), label-free quantitative mass spectrometry iScience Medium 31476617
2019 SBP1 accumulates in electron-dense material (EDM) in the parasite cytoplasm during the early trophozoite (ring form) stage and is subsequently found in the parasitophorous vacuolar (PV) space before translocation to Maurer's clefts, defining an intermediate trafficking step for SBP1 export. Immunoelectron microscopy with anti-SBP1 antibodies raised against recombinant PfSBP1 Parasitology international Medium 31669509
2023 SBP1 and MAHRP2 assume a lumenal topology within the parasite secretory pathway (ER lumen), forming ER-lumenal intermediates during export; addition of a C-terminal KDEL ER-retention sequence enhanced retention of SBP1 in the parasite ER, indicating that a sub-population of SBP1 adopts an ER-lumenal state that is a productive intermediate in the export process. SBP1 is targeted by an internal hydrophobic sequence that, unlike a transmembrane segment, does not span the ER membrane. Chimeric reporter constructs with ER-retention sequences, intact-cell topology assays, fluorescence microscopy, mass spectrometry PLoS pathogens Medium 37000891
2024 SBP1 is expressed in gametocyte-infected erythrocytes and localizes to dot-like Maurer's cleft structures in their cytoplasm; co-immunoprecipitation followed by mass spectrometry identified PfHSP70-1 and PfHSP70-x as SBP1-interacting molecular chaperones in gametocyte-infected erythrocytes, with some HSP70 co-localizing in a dot-like cytoplasmic pattern in immature gametocytes. Co-immunoprecipitation, mass spectrometry, immunofluorescence localization in gametocyte-infected erythrocytes Parasitology international Medium 38331312
2018 Direct in vitro interaction was demonstrated between purified PfSBP1 and recombinant PfJ23 (a PEXEL-positive hyp16 family member); PfJ23, PfSBP1 and PfEMP1 can form a tripartite complex in vitro, and PfJ23 partially co-localizes with PfSBP1 in parasite-infected erythrocytes. In vitro pulldown with recombinant proteins, co-immunoprecipitation with native proteins, immunofluorescence co-localization Pathogens and disease Low 30576479
2019 The cytoplasmic domain of CBP2 (cCBP2) interacts in vitro with PfSBP1; this interaction is influenced by ATP binding to cCBP2, which induces structural changes in the protein. In vitro binding assay with recombinant proteins, biophysical characterization International journal of biological macromolecules Low 31356937
2021 SBP1 KO P. berghei parasites (lacking sequestration ability) induced similar early lung pathology as wild-type parasites in experimental MA-ARDS, but lung pathology resolved in >60% of SBP1 KO-infected mice, associated with decreased inflammatory cytokine expression and lower cytotoxic CD8+ T cell markers; this establishes that SBP1-mediated sequestration inhibits spontaneous disease resolution rather than being required for initial pathology. SBP1 KO P. berghei in vivo mouse model, bioluminescence imaging, RT-qPCR (parasite load and cytokines), flow cytometry for CD8+ T cells, histopathology PLoS pathogens Medium 34843584

Source papers

Stage 0 corpus · 35 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2000 Pfsbp1, a Maurer's cleft Plasmodium falciparum protein, is associated with the erythrocyte skeleton. Molecular and biochemical parasitology 195 11087921
2006 A Maurer's cleft-associated protein is essential for expression of the major malaria virulence antigen on the surface of infected red blood cells. The Journal of cell biology 152 16520384
2006 Skeleton-binding protein 1 functions at the parasitophorous vacuole membrane to traffic PfEMP1 to the Plasmodium falciparum-infected erythrocyte surface. Blood 137 17023587
2013 Role of plasmepsin V in export of diverse protein families from the Plasmodium falciparum exportome. Traffic (Copenhagen, Denmark) 108 23387285
2008 Sequence requirements for the export of the Plasmodium falciparum Maurer's clefts protein REX2. Molecular microbiology 71 19170882
2016 The machinery underlying malaria parasite virulence is conserved between rodent and human malaria parasites. Nature communications 60 27225796
2008 Export of PfSBP1 to the Plasmodium falciparum Maurer's clefts. Traffic (Copenhagen, Denmark) 59 19054387
2006 Protein phosphatase 1, a Plasmodium falciparum essential enzyme, is exported to the host cell and implicated in the release of infectious merozoites. Cellular microbiology 40 16548885
2005 LANCL1, an erythrocyte protein recruited to the Maurer's clefts during Plasmodium falciparum development. Molecular and biochemical parasitology 34 15811525
2015 Interactions between Plasmodium falciparum skeleton-binding protein 1 and the membrane skeleton of malaria-infected red blood cells. Biochimica et biophysica acta 26 25883090
2008 A conditional export system provides new insights into protein export in Plasmodium falciparum-infected erythrocytes. Cellular microbiology 26 18691247
2017 Molecular Markers for Sensitive Detection of Plasmodium falciparum Asexual Stage Parasites and their Application in a Malaria Clinical Trial. The American journal of tropical medicine and hygiene 24 28719294
2011 Amplification of P. falciparum Cytoadherence through induction of a pro-adhesive state in host endothelium. PloS one 22 22043276
2016 A single point in protein trafficking by Plasmodium falciparum determines the expression of major antigens on the surface of infected erythrocytes targeted by human antibodies. Cellular and molecular life sciences : CMLS 20 27193441
2016 Plasmodium knowlesi Skeleton-Binding Protein 1 Localizes to the 'Sinton and Mulligan' Stipplings in the Cytoplasm of Monkey and Human Erythrocytes. PloS one 16 27732628
2017 PHISTc protein family members localize to different subcellular organelles and bind Plasmodium falciparum major virulence factor PfEMP-1. The FEBS journal 15 29155505
2015 New Export Pathway in Plasmodium falciparum-Infected Erythrocytes: Role of the Parasite Group II Chaperonin, PfTRiC. Traffic (Copenhagen, Denmark) 15 25615740
2010 Functional evaluation of Plasmodium export signals in Plasmodium berghei suggests multiple modes of protein export. PloS one 15 20419102
2019 Plasmodium falciparum Gametocyte Enrichment in Peripheral Blood Samples by Magnetic Fractionation: Gametocyte Yields and Possibilities to Reuse Columns. The American journal of tropical medicine and hygiene 13 30608048
2023 Time-resolved proximity biotinylation implicates a porin protein in export of transmembrane malaria parasite effectors. Journal of cell science 11 37772444
2022 Experimental malaria-associated acute kidney injury is independent of parasite sequestration and resolves upon antimalarial treatment. Frontiers in cellular and infection microbiology 11 36004329
2021 Skeleton binding protein-1-mediated parasite sequestration inhibits spontaneous resolution of malaria-associated acute respiratory distress syndrome. PLoS pathogens 11 34843584
2019 A High-Resolution Map of SBP1 Interactomes in Plasmodium falciparum-infected Erythrocytes. iScience 11 31476617
2018 Comparative genomics and proteomic analyses between lethal and nonlethal strains of Plasmodium berghei. Experimental parasitology 8 29307564
2024 Persistent and multiclonal malaria parasite dynamics despite extended artemether-lumefantrine treatment in children. Nature communications 7 38714692
2019 Skeleton binding protein 1 (SBP1) of Plasmodium falciparum accumulates in electron-dense material before passing through the parasitophorous vacuole membrane. Parasitology international 7 31669509
2006 Deciphering the export pathway of malaria surface proteins. Trends in parasitology 7 16843728
2025 Isolation and characterization of Plasmodium falciparum blood-stage persisters by improved selection protocols using dihydroartemisinin alone. Antimicrobial agents and chemotherapy 5 39927767
2021 Persistence of mRNA indicative of Plasmodium falciparum ring-stage parasites 42 days after artemisinin and non-artemisinin combination therapy in naturally infected Malians. Malaria journal 5 33422068
2023 Formation of ER-lumenal intermediates during export of Plasmodium proteins containing transmembrane-like hydrophobic sequences. PLoS pathogens 4 37000891
2018 Plasmodium falciparum protein 'PfJ23' hosts distinct binding sites for major virulence factor 'PfEMP1' and Maurer's cleft marker 'PfSBP1'. Pathogens and disease 3 30576479
2024 Transcriptional responses of brain endothelium to Plasmodium falciparum patient-derived isolates in vitro. Microbiology spectrum 1 38864616
2019 CX3CL1 binding protein-2 (CBP2) of Plasmodium falciparum binds nucleic acids. International journal of biological macromolecules 1 31356937
2024 Skeleton binding protein 1 localizes to the Maurer's cleft and interacts with PfHSP70-1 and PfHSP70-x in Plasmodium falciparum gametocyte-infected erythrocytes. Parasitology international 0 38331312
2020 [Method for rapid synchronization of different growth cycles of Plasmodium falciparum in vitro and application in differential gene expression profile of 3D7 after dihydroartemisinin treatment]. Zhongguo Zhong yao za zhi = Zhongguo zhongyao zazhi = China journal of Chinese materia medica 0 32495606