Affinage · Plasmodium

EXP2

PF3D7_1471100 · exported protein 2

Annotated
2026-09-08
41 papers in source corpus 28 papers cited in narrative 28 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

EXP2 (PF3D7_1471100) is the membrane-spanning, pore-forming subunit of the Plasmodium translocon of exported proteins (PTEX) at the parasitophorous vacuole membrane (PVM), where it forms a core complex with PTEX150 and the AAA+ ATPase HSP101 that drives export of parasite proteins into the host erythrocyte (PMID:19536257, PMID:30150771). Near-atomic cryo-EM of the endogenous complex shows that EXP2 and PTEX150 interdigitate into a static, funnel-shaped pseudo-seven-fold-symmetric protein-conducting channel spanning the vacuolar membrane, over which the HSP101 hexamer is tethered and undergoes conformational cycling to thread cargo (PMID:30150771); consistent with this, exported proteins arrested during translocation are trapped in complex with EXP2 at the PVM, clogging the pore and blocking export (PMID:27168322, PMID:23361006). Recombinant EXP2 self-assembles into ~10–12-subunit pores in lipid bilayers, and its protease-resistant, membrane-associated N-terminal ~20 kDa region (bearing a C113–C140 intramolecular disulfide bond) forms the transmembrane, pore-forming element with the C-terminus projecting into the vacuolar space (PMID:27865834, PMID:30476118). Beyond protein export, EXP2 independently serves as a nutrient-permeable channel across the PVM, a function that requires EXP1 for its correct localization and organization but is separable from HSP101-dependent export (PMID:30150733, PMID:31568532, PMID:31990132). EXP2 is essential across the life cycle: it is required for blood-stage growth and protein export (PMID:30439948), for intrahepatic liver-stage development (PMID:26347246, PMID:36445080, PMID:38968107), and for hepatocyte invasion by sporozoites, where its pore-forming activity triggers host membrane repair that facilitates entry (PMID:33159090).

Mechanistic history

Synthesis pass · year-by-year structured walk · 13 steps
  1. 1994 Medium

    Establishing that EXP2 is a bona fide PVM-associated membrane protein was the prerequisite for any functional role at the host-parasite interface.

    Evidence Monoclonal antibody characterization, biochemical fractionation, and immunolocalization in P. falciparum

    PMID:8058359

    Open questions at the time
    • Function of the PVM association not addressed
    • No oligomeric or channel activity tested
  2. 1998 Medium

    Cloning showed EXP2 is a single-copy, ring-stage gene with a cleaved signal sequence and no canonical transmembrane domain, raising the question of how it inserts into the PVM.

    Evidence Gene cloning, sequencing, N-terminal microsequencing, and hydrophobicity analysis in P. falciparum

    PMID:9574909

    Open questions at the time
    • Membrane-association mode inferred (amphipathic helix), not experimentally demonstrated
    • No functional assay of the protein
  3. 2009 High

    Discovery of PTEX defined EXP2 as the membrane-associated component of an ATP-powered export machine, placing it at the center of protein trafficking into the host cell.

    Evidence Co-IP, mass spectrometry, biochemical fractionation, and immunolocalization identifying the EXP2–PTEX150–HSP101 core in P. falciparum

    PMID:19536257

    Open questions at the time
    • Whether EXP2 itself conducts cargo not yet shown
    • Stoichiometry and structure of the channel unknown
  4. 2012 High

    Tracing EXP2's biogenesis showed it is made early, stored in merozoite dense granules, and forms a stable ~600 kDa homo-oligomer at the PVM upstream of the other PTEX subunits, defining an assembly order.

    Evidence Pulse-chase, fractionation, native PAGE, and detergent separation in P. falciparum

    PMID:22253438

    Open questions at the time
    • Homo-oligomer architecture not resolved
    • Nature of EXP2–PTEX150–HSP101 coupling not defined at molecular level
  5. 2013 Medium

    Failure to delete exp2 in P. berghei established that EXP2 is essential for blood-stage development, motivating conditional approaches.

    Evidence Repeated failed gene knockout attempts in P. berghei (two independent studies)

    PMID:23869529 PMID:24076174

    Open questions at the time
    • Essentiality is a negative genetic result without mechanistic cause
    • Life-cycle stages beyond blood not addressed here
  6. 2013 High

    Super-resolution imaging placed protein export spatially at PVM foci containing EXP2, providing direct cellular evidence that translocation occurs where PTEX resides.

    Evidence 3D-SIM, live merozoite imaging, and translocation intermediate generation in P. falciparum

    PMID:23361006

    Open questions at the time
    • Does not show EXP2 physically conducting cargo
    • Dynamics of foci formation not mechanistically explained
  7. 2015 High

    Conditional deletion and tagging in P. berghei extended EXP2's essential role beyond blood stage to liver growth and transition to blood-stage infection, and revealed dynamic tubular PVM extensions consistent with pore activity.

    Evidence FLP/FRT conditional mutagenesis, mouse infection, and endogenous fluorescent tagging with CLEM in P. berghei; vesicle localization noted in P. yoelii reticulocytes

    PMID:25662767 PMID:26219962 PMID:26347246

    Open questions at the time
    • Molecular basis of liver-stage requirement not defined
    • Species-divergent cytoplasmic vesicle localization in P. yoelii reticulocytes not mechanistically explained
  8. 2016 High

    Trapping stalled cargo in complex with EXP2 gave the first functional proof that EXP2 is part of the translocating entity, and reconstitution showed EXP2 alone forms a defined pore.

    Evidence DHFR conditional-fold constructs with Co-IP of intermediates and growth assays; recombinant EXP2 pore reconstitution by bilayer electrophysiology, EM, SEC, and BN-PAGE in P. falciparum

    PMID:27168322 PMID:27865834

    Open questions at the time
    • Recombinant pore stoichiometry (~10–12) differs from later cryo-EM channel; reconciliation not resolved
    • Two-step export across PPM and PVM mechanistically defined only in outline
  9. 2018 High

    Cryo-EM, conditional knockdown, and electrophysiology together defined the channel architecture and split EXP2's activities into an HSP101-dependent protein-export channel and an HSP101-independent nutrient channel.

    Evidence Near-atomic cryo-EM of endogenous PTEX; TetR-aptamer/glmS knockdown, patch-clamp, mutagenesis, and export assays; SIM of EXP2 loop extensions in P. falciparum

    PMID:29696751 PMID:30150733 PMID:30150771 PMID:30439948

    Open questions at the time
    • How the same channel switches between nutrient and protein conduction not resolved
    • Gating and selectivity mechanisms not defined
  10. 2019 High

    Biochemical topology mapping and EXP1 knockout dissected which part of EXP2 forms the pore and which partner controls its nutrient-channel function.

    Evidence Differential alkylation, protease protection, hemolysis and osmotic protection with synthetic peptide; conditional EXP1 KO with patch-clamp and export assays in P. falciparum

    PMID:30476118 PMID:31568532

    Open questions at the time
    • Molecular mechanism by which EXP1 organizes EXP2 not defined
    • Whether EXP1 acts stoichiometrically or as a chaperone unclear
  11. 2020 High

    Localization studies refined EXP2's PVM organization—dependent on EXP1 and excluded from PVM/PPM contact domains—while a new role emerged in sporozoite invasion via pore-induced host membrane repair.

    Evidence CRISPR/Cpf1 EXP1 knockdown with BioID2 and EM; super-resolution imaging of contact domains; sporozoite deletion with recombinant EXP2/alpha-hemolysin/acid sphingomyelinase rescue in P. falciparum

    PMID:31990132 PMID:32732874 PMID:33159090

    Open questions at the time
    • Mechanistic link between EXP2 pore activity and membrane-repair signaling at hepatocyte surface incompletely defined
    • Functional consequence of EXP2 exclusion from contact domains unknown
  12. 2022 Medium

    Further studies defined an EXP2–PTEX150 subcomplex as the HSP101 docking platform and demonstrated a liver-stage requirement for EXP2 separable from invasion.

    Evidence Fractionation and Co-IP of the EXP2–PTEX150 subcomplex; postinvasion glmS knockdown in P. berghei with LISP2 marker and luciferase readouts

    PMID:35192672 PMID:36445080

    Open questions at the time
    • Subcomplex assembly demonstrated by Co-IP only
    • Liver-stage export cargo dependence not fully enumerated
  13. 2024 High

    Complementation and conditional sporozoite disruption defined EXP2's body region as critical for PTEX assembly, showed a heterologous ortholog cannot substitute, and confirmed EXP2 is essential for intrahepatic growth after successful invasion.

    Evidence Transgenic complementation with truncations/hybrids/GRA17 and export/growth assays; FlpL/FRT sporozoite disruption with humanized-mouse liver-stage model in P. falciparum; knockER ER-sequestration

    PMID:37552754 PMID:38282616 PMID:38968107

    Open questions at the time
    • Why GRA17 fails to complement despite structural orthology not fully explained
    • Precise cargo set required for liver-stage growth incomplete

Open questions

Synthesis pass · forward-looking unresolved questions
  • How EXP2 mechanistically toggles between HSP101-driven protein translocation and HSP101-independent nutrient conduction within a single static channel, and how EXP1 physically organizes it, remains unresolved.
  • No structure of the nutrient-conducting (HSP101-free) state
  • Gating/selectivity switch between the two modes undefined
  • Molecular mechanism of EXP1-dependent organization of EXP2 unknown

Mechanism profile

Synthesis pass · controlled-vocabulary classification
Partners
EXP1 (REQUIRED FOR EXP2 PVM ORGANIZATION AND NUTRIENT-CHANNEL ACTIVITY)HSP101PTEX150
Complex memberships
EXP2 ~600 kDa homo-oligomerEXP2–PTEX150 static channel subcomplexPTEX translocon core complex (EXP2–PTEX150–HSP101)

Evidence

Reading pass · 28 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2009 EXP2 was identified as the membrane-associated, pore-forming component of the PTEX (Plasmodium translocon of exported proteins) complex, which is located in the parasitophorous vacuole membrane (PVM) and is ATP-powered. EXP2 forms part of a core complex with HSP101 and PTEX150. Co-immunoprecipitation, mass spectrometry, biochemical fractionation, and immunolocalization Nature High 19536257
1994 EXP2 (35 kDa protein) was identified as a membrane protein tightly associated with the parasitophorous vacuole membrane and membrane-bound compartments in the infected erythrocyte cytoplasm, resistant to alkali extraction but soluble in detergent, and co-localizing with EXP1. Monoclonal antibody characterization, biochemical fractionation, immunolocalization Parasitology Medium 8058359
1998 EXP2 gene was cloned and characterized: it is encoded by a single-copy gene on chromosome 14, transcribed during the ring stage, contains an N-terminal signal sequence that is cleaved from the mature protein, and lacks a typical hydrophobic transmembrane domain. EXP2 may associate with the vacuolar membrane via an amphipathic helix in the N-terminal half. Gene cloning, PCR, cDNA/genomic sequencing, N-terminal microsequencing, hydrophobicity analysis Molecular and biochemical parasitology Medium 9574909
2012 EXP2 is synthesized earlier in the life cycle than other PTEX components (HSP101 and PTEX150), resides in dense granules of invasive merozoites, and is released into the host cell upon invasion to reside in the PVM with little turnover. EXP2 forms an ~600 kDa apparently homo-oligomeric complex that can be separated from HSP101 and PTEX150 using non-ionic detergents, and biochemical evidence supports an EXP2–PTEX150–HSP101 association order with EXP2 at the vacuolar membrane. Pulse-chase labeling, immunofluorescence, subcellular fractionation, native gel electrophoresis, non-ionic detergent separation The Journal of biological chemistry High 22253438
2013 EXP2, PTEX150, and HSP101 could not be genetically deleted in Plasmodium berghei, consistent with essential roles during blood-stage development. Repeated gene deletion attempts (genetic knockout) in P. berghei Molecular microbiology Medium 23869529
2013 Repeated attempts to delete exp2 in Plasmodium berghei failed, suggesting EXP2 performs an essential function during blood-stage development. Gene deletion attempts in P. berghei Molecular and biochemical parasitology Medium 24076174
2013 Three-dimensional structured illumination microscopy showed that EXP2, as part of PTEX complexes, localizes in dynamic foci at the PVM and that exported proteins spatially associate with EXP2 during both native conditions and upon generation of translocation intermediates, providing direct cellular evidence that protein export occurs at PVM regions housing PTEX. 3D structured illumination microscopy (3D-SIM), live imaging of purified merozoites, translocation intermediate generation Nature communications High 23361006
2015 Conditional deletion of EXP2 using the FLP/FRT system in P. berghei showed that EXP2 is important for parasite growth in the liver and critical for transition to blood-stage infection. EXP2-deficient parasites were severely impaired in generating patent blood-stage infection. FLP/FRT conditional mutagenesis, mouse infection experiments Cellular microbiology High 26347246
2015 In P. berghei, fluorescent tagging of EXP2 revealed its prominent presence at the parasite periphery and in motile, tubular extensions of the parasitophorous vacuole that protrude far into the red blood cell, consistent with EXP2's proposed role in pore formation. Endogenous fluorescent tagging, live cell imaging, correlative light and electron microscopy Scientific reports Medium 26219962
2015 In P. yoelii-infected reticulocytes, EXP2 localizes not only to the PVM but also to distinct membrane-bound vesicles in the reticulocyte cytoplasm, in contrast to P. falciparum in mature RBCs where EXP2 is exclusively at the PVM. This cytoplasmic vesicle localization was primarily seen in CD71+ reticulocytes versus mature RBCs, and the pyexp2 gene was refractory to deletion. Immunofluorescence, proteomic screen, transgenic HA-tagging, conditional deletion attempts Eukaryotic cell Medium 25662767
2016 Constructs of exported proteins arrested during translocation across the PVM were found in complex with EXP2, providing the first functional evidence that EXP2 is part of a translocating entity at the PVM. Clogging of the translocation pore by these stable intermediates prevented export of all exported protein types and inhibited parasite growth. Two successive translocation steps (one at the parasite plasma membrane and one at the PVM) are required for transmembrane protein export. Conditionally foldable domain (DHFR) constructs, co-immunoprecipitation of translocation intermediates with EXP2, parasite growth assays PLoS pathogens High 27168322
2016 Recombinant EXP2 expressed in E. coli (as a GST fusion) forms pores in bilayer lipid membranes. The inner pore diameter is approximately 3.5 nm based on electron microscopy and channel current measurements. The pore comprises approximately 10–12 EXP2 subunits as determined by size exclusion chromatography and blue native PAGE. Recombinant protein expression, bilayer lipid membrane electrophysiology, electron microscopy, size exclusion chromatography, blue native PAGE Biochemical and biophysical research communications High 27865834
2018 Cryo-electron microscopy structures of the endogenous PTEX core complex at near-atomic resolution showed that EXP2 and PTEX150 interdigitate to form a static, funnel-shaped pseudo-seven-fold-symmetric protein-conducting channel spanning the vacuolar membrane. EXP2 and PTEX150 form the static channel component, while the AAA+ HSP101 hexamer is tethered above this funnel and undergoes conformational changes for cargo threading. Cryo-electron microscopy, CRISPR-Cas9 epitope tagging for endogenous complex isolation, structural analysis of 'engaged' and 'resetting' states Nature High 30150771
2018 Using regulated gene expression (TetR-aptamer knockdown), mutagenesis, and cell-attached patch-clamp electrophysiology, EXP2 was shown to serve dual roles: as a protein-conducting channel in the context of PTEX and as a channel facilitating nutrient passage across the PVM independent of HSP101. TetR-aptamer conditional knockdown, patch-clamp electrophysiology, mutagenesis, protein export assays Nature microbiology High 30150733
2018 Inducible knockdown of EXP2 in P. falciparum blood stages strongly reduced parasite growth proportional to degree of knockdown, stalled development midway through the asexual cycle, and caused severe attenuation of protein export of a tracked exported protein. Growth recovered upon restoration of EXP2 expression. Inducible knockdown (glmS ribozyme system), parasite growth assays, exported protein trafficking assay PloS one High 30439948
2018 When cargo proteins were trapped at the parasite surface, loop-like extensions appeared at the PVM containing both trapped cargo and EXP2, but not HSP101 or PTEX150, suggesting EXP2 can be redistributed to these extensions independently of the full PTEX complex. DHFR-based export block, structured illumination microscopy, immunofluorescence Traffic (Copenhagen, Denmark) Medium 29696751
2019 Biochemical analysis of EXP2 revealed that cysteines C113 and C140 form an intramolecular disulfide bond while C201 is predominantly reduced. EXP2 has a protease-resistant, membrane-associated N-terminal region (~20 kDa) that does not project into the erythrocyte cytosol, while its C-terminus projects into the vacuole space. A transmembrane peptide from the N-terminal region is hemolytic and forms a discrete pore in an osmotic protection assay. Differential alkylation, protease protection assay, hemolysis assay, osmotic protection assay with synthetic peptide Journal of biochemistry High 30476118
2019 Loss of EXP1 caused loss of correct localization of EXP2 at the PVM and abolished the nutrient-permeable channel activity of the PVM without affecting protein export, demonstrating that EXP1 is specifically required for functional expression of EXP2 as the nutrient-permeable channel. Conditional EXP1 knockout, patch-clamp electrophysiology, protein export assays, immunofluorescence PLoS biology High 31568532
2020 EXP1 knockdown substantially altered the distribution of EXP2 within the PVM but did not impact the distribution of HSP101, revealing that EXP1 is required for proper organization of EXP2 within the PVM. CRISPR/Cpf1-mediated conditional knockdown (TetR-DOZI-aptamers), BioID2 proximity labeling, immunofluorescence, electron microscopy Cellular microbiology High 31990132
2020 EXP2 is excluded from micrometer-sized contact sites of close apposition between the PVM and parasite plasma membrane (contacting domains), while the lipid transporter PfNCR1 is included in these regions, demonstrating spatial segregation of the hydrophilic nutrient/protein channel EXP2 from a hydrophobic substrate transporter. Super-resolution fluorescence microscopy, electron microscopy, subcellular localization of tagged proteins Nature communications Medium 32732874
2020 EXP2 is a pore-forming protein secreted from sporozoites upon contact with the host cell milieu, and EXP2 is critical for hepatocyte invasion. EXP2-deficient sporozoites are impaired in invasion, rescued by exogenous recombinant EXP2 or alpha-hemolysin (a pore-forming protein), and by acid sphingomyelinase, indicating that EXP2's pore-forming activity induces hepatocyte membrane repair, which facilitates parasite invasion. Genetic deletion, recombinant protein rescue, chemical inhibition and genetic knockdown of acid sphingomyelinase, invasion assays Nature communications High 33159090
2021 EXP2 forms part of a translocation intermediate complex with core PTEX components (HSP101 and PTEX150) during export of the integral membrane protein SURFIN4.1 (mini-SURFIN4.1). A processed form of Pf113 also associates with EXP2 in stable translocation intermediates at the parasite plasma membrane. Co-immunoprecipitation of translocation intermediates, structured illumination microscopy Parasitology international Medium 33901679
2022 EXP2 and PTEX150 form a stable subcomplex that facilitates HSP101 docking onto PTEX. This EXP2-PTEX150 subcomplex is a functional assembly unit within the translocon. Biochemical fractionation, co-immunoprecipitation, immunofluorescence showing HSP101 in parasite ER and PV PLoS pathogens Medium 35192672
2022 Postinvasion knockdown of EXP2 using the glmS ribozyme in P. berghei reduced parasite size during intrahepatic development and largely abolished expression of the mid-to-late liver-stage marker LISP2, demonstrating that EXP2 is important for intrahepatic parasite development independently of its role in invasion. glmS ribozyme-mediated conditional knockdown after hepatocyte invasion, immunofluorescence, nanoluciferase reporter assays mBio High 36445080
2023 ER sequestration (knockER) of EXP2 using inducible KDEL fusion demonstrated that EXP2 can be redistributed from the PV to the ER, establishing EXP2's secretory pathway trafficking and enabling loss-of-function studies for vacuolar EXP2. DiCre-mediated inducible KDEL ER-retrieval (knockER), fluorescence microscopy, parasite growth assays Proceedings of the National Academy of Sciences of the United States of America Medium 37552754
2024 Complementation assays in EXP2 knockdown P. falciparum parasites showed that T. gondii GRA17 (a structural ortholog) cannot complement EXP2's protein export function even when supplemented with EXP2's assembly strand and linker helix. The body region of EXP2 is critical for PTEX assembly and/or EXP2 insertion efficiency into the PVM. Altering timing and abundance of EXP2 expression did not affect protein export but affected parasite viability, indicating EXP2's unique transcriptional profile enables its additional nutrient exchange role. Transgenic complementation with truncations, hybrids, and heterologous GRA17; protein export assays; parasite growth assays Frontiers in cellular and infection microbiology High 38282616
2024 FlpL/FRT-mediated disruption of exp2 in P. falciparum sporozoites did not affect sporozoite development in mosquitoes or infectivity of hepatocytes but caused 100% loss of liver parasites by day 6 post-infection, demonstrating that EXP2 is essential for intrahepatic liver-stage growth. Expression of some PEXEL proteins (LISP2, CSP but not LSA3) was reduced in exp2-FRT liver stages. FlpL/FRT conditional gene excision in sporozoites, humanized mouse liver-stage infection model, immunofluorescence of PEXEL reporter proteins Proceedings of the National Academy of Sciences of the United States of America High 38968107
2026 An EXP2-fluorescent reporter was used to track PVM integrity during egress, showing that the PVM ruptures at a single site and the rupture rapidly expands from that initial site, releasing merozoites. EXP2 localization allowed real-time monitoring of PVM breakdown relative to exocytosis and RBC membrane rupture. Live fluorescence imaging of EXP2-fluorescent fusion during egress, conditional mutants of PfERC PLoS pathogens Low 42113900

Source papers

Stage 0 corpus · 41 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2009 A newly discovered protein export machine in malaria parasites. Nature 381 19536257
2014 PTEX component HSP101 mediates export of diverse malaria effectors into host erythrocytes. Nature 205 25043010
2012 Complete Plasmodium falciparum liver-stage development in liver-chimeric mice. The Journal of clinical investigation 187 22996664
2018 Malaria parasite translocon structure and mechanism of effector export. Nature 159 30150771
2012 Biosynthesis, localization, and macromolecular arrangement of the Plasmodium falciparum translocon of exported proteins (PTEX). The Journal of biological chemistry 120 22253438
2018 EXP2 is a nutrient-permeable channel in the vacuolar membrane of Plasmodium and is essential for protein export via PTEX. Nature microbiology 92 30150733
2016 Stable Translocation Intermediates Jam Global Protein Export in Plasmodium falciparum Parasites and Link the PTEX Component EXP2 with Translocation Activity. PLoS pathogens 76 27168322
2013 Spatial association with PTEX complexes defines regions for effector export into Plasmodium falciparum-infected erythrocytes. Nature communications 75 23361006
2013 The Plasmodium translocon of exported proteins (PTEX) component thioredoxin-2 is important for maintaining normal blood-stage growth. Molecular microbiology 72 23869529
2013 Two putative protein export regulators promote Plasmodium blood stage development in vivo. Molecular and biochemical parasitology 66 24076174
2019 EXP1 is critical for nutrient uptake across the parasitophorous vacuole membrane of malaria parasites. PLoS biology 61 31568532
1994 Characterization of membrane proteins exported from Plasmodium falciparum into the host erythrocyte. Parasitology 53 8058359
2020 EXP1 is required for organisation of EXP2 in the intraerythrocytic malaria parasite vacuole. Cellular microbiology 47 31990132
2015 The Plasmodium berghei translocon of exported proteins reveals spatiotemporal dynamics of tubular extensions. Scientific reports 39 26219962
2015 The Plasmodium translocon of exported proteins component EXP2 is critical for establishing a patent malaria infection in mice. Cellular microbiology 36 26347246
2018 Knockdown of the translocon protein EXP2 in Plasmodium falciparum reduces growth and protein export. PloS one 31 30439948
2018 Spatial organization of protein export in malaria parasite blood stages. Traffic (Copenhagen, Denmark) 29 29696751
2020 Contacting domains segregate a lipid transporter from a solute transporter in the malarial host-parasite interface. Nature communications 28 32732874
2018 PV1, a novel Plasmodium falciparum merozoite dense granule protein, interacts with exported protein in infected erythrocytes. Scientific reports 28 29487358
1998 Characterization and cloning of the gene encoding the vacuolar membrane protein EXP-2 from Plasmodium falciparum. Molecular and biochemical parasitology 28 9574909
2019 Deletion of Plasmodium falciparum Protein RON3 Affects the Functional Translocation of Exported Proteins and Glucose Uptake. mBio 25 31289187
2016 Expression and characterization of the Plasmodium translocon of the exported proteins component EXP2. Biochemical and biophysical research communications 23 27865834
2022 A revised mechanism for how Plasmodium falciparum recruits and exports proteins into its erythrocytic host cell. PLoS pathogens 19 35192672
2019 Latent transcriptional variations of individual Plasmodium falciparum uncovered by single-cell RNA-seq and fluorescence imaging. PLoS genetics 18 31856180
2015 Host erythrocyte environment influences the localization of exported protein 2, an essential component of the Plasmodium translocon. Eukaryotic cell 17 25662767
2020 Plasmodium translocon component EXP2 facilitates hepatocyte invasion. Nature communications 15 33159090
2007 Characterization of Maurer's clefts in Plasmodium falciparum-infected erythrocytes. The American journal of tropical medicine and hygiene 15 17255224
2019 The N-terminus of EXP2 forms the membrane-associated pore of the protein exporting translocon PTEX in Plasmodium falciparum. Journal of biochemistry 14 30476118
2022 Heme Detoxification Protein (PfHDP) is essential for the hemoglobin uptake and metabolism in Plasmodium falciparum. FASEB bioAdvances 10 36238365
2022 The PTEX Pore Component EXP2 Is Important for Intrahepatic Development during the Plasmodium Liver Stage. mBio 10 36445080
2023 Knock-sideways by inducible ER retrieval enables a unique approach for studying Plasmodium-secreted proteins. Proceedings of the National Academy of Sciences of the United States of America 9 37552754
2021 Plasmodium falciparum SURFIN4.1 forms an intermediate complex with PTEX components and Pf113 during export to the red blood cell. Parasitology international 9 33901679
2024 Flp/FRT-mediated disruption of ptex150 and exp2 in Plasmodium falciparum sporozoites inhibits liver-stage development. Proceedings of the National Academy of Sciences of the United States of America 8 38968107
2022 A member of the tryptophan-rich protein family is required for efficient sequestration of Plasmodium berghei schizonts. PLoS pathogens 8 36126089
2016 An external sensing system in Plasmodium falciparum-infected erythrocytes. Malaria journal 7 26893139
2025 Redesign of Translocon EXP2 Nanopore for Detecting Peptide Fragments. Small methods 6 39905884
2023 NK cell-induced damage to P.falciparum-infected erythrocytes requires ligand-specific recognition and releases parasitophorous vacuoles that are phagocytosed by monocytes in the presence of immune IgG. PLoS pathogens 4 37939134
2022 Mid-Liver Stage Arrest of Plasmodium falciparum Schizonts in Primary Porcine Hepatocytes. Frontiers in cellular and infection microbiology 4 35252038
2020 Synthetic DNA Vaccines Adjuvanted with pIL-33 Drive Liver-Localized T Cells and Provide Protection from Plasmodium Challenge in a Mouse Model. Vaccines 4 31936739
2024 Dissecting EXP2 sequence requirements for protein export in malaria parasites. Frontiers in cellular and infection microbiology 2 38282616
2026 Spatiotemporal dynamics of signal dependent exocytosis and parasitophorous vacuolar membrane rupture during Plasmodium falciparum egress. PLoS pathogens 1 42113900