Affinage · Plasmodium

EXP1

PF3D7_1121600 · exported protein 1

Annotated
2026-09-08
69 papers in source corpus 24 papers cited in narrative 25 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

EXP1 (PF3D7_1121600) is an essential, single-pass integral membrane protein of the parasitophorous vacuole membrane (PVM) that is required for nutrient acquisition by intraerythrocytic Plasmodium parasites (PMID:31568532). It is synthesized as a ~23 kDa protein bearing an N-terminal signal sequence and an internal hydrophobic anchor, and adopts a defined single-pass topology with its N-terminus in the vesicle lumen and its C-terminus exposed to the cytoplasmic face (PMID:2410913, PMID:1852170). Its signal sequence actively engages the ER translocation machinery and directs the protein along the default secretory route to the parasitophorous vacuole (PMID:12456681, PMID:10645548), with trafficking to the PVM occurring independently of the PTEX protein-export translocon and independent of the folding state of the protein (PMID:27892646). In P. falciparum merozoites, EXP1 is first stored in dense granules and is translocated to the PVM after erythrocyte invasion (PMID:29886341), where it forms oligomeric arrays that occupy microdomains distinct from those of ETRAMP family proteins (PMID:16420351, PMID:12686607). Conditional knockout demonstrates that EXP1 is required for the correct organization and function of EXP2 as the PVM nutrient-permeable channel: loss of EXP1 abolishes channel activity measured by patch-clamp and renders parasites hypersensitive to low nutrient conditions, while leaving PTEX-mediated protein export intact (PMID:31568532, PMID:31990132). A previously proposed membrane glutathione S-transferase activity that degrades hematin and is inhibited by artesunate (PMID:25126794) does not account for the essential in vivo function of EXP1, since conditional knockdown recapitulates the essential phenotype independently of GST activity (PMID:31990132). In liver stages, the C-terminal domain of EXP1 binds host Apolipoprotein H and is required for correct PVM localization and intrahepatic development, as shown in P. berghei by truncation mutants and host ApoH knockdown (PMID:28137845, PMID:31364224).

Mechanistic history

Synthesis pass · year-by-year structured walk · 10 steps
  1. 1987 Medium

    Establishing that EXP1 is exported beyond the parasite into a new host-cell compartment defined it as a secreted/exported antigen and raised the question of its destination and function.

    Evidence Monoclonal antibody localization plus gene cloning and sequencing in P. falciparum

    PMID:2410913 PMID:2438130

    Open questions at the time
    • Precise membrane compartment not yet resolved
    • Molecular function unknown
  2. 1991 High

    Determining that EXP1 is an integral membrane protein with a fixed single-pass topology (N-terminus luminal, C-terminus exposed) set the structural framework for how its two domains face different environments.

    Evidence Cell-free translation/translocation into microsomes with proteinase K protection, alkaline extraction, and segment-specific antibodies in P. falciparum

    PMID:1852170

    Open questions at the time
    • Function of each domain not established
    • Oligomeric state in native membrane not addressed
  3. 1994 Medium

    Pinpointing EXP1 to the PVM and to exported membrane networks (TVN/tubovesicular membrane) — and showing it segregates from other exported proteins and co-resides with EXP-2 — localized the protein to its site of action and hinted at organized membrane microdomains.

    Evidence Monoclonal antibody co-localization, membrane fractionation, and confocal lipid/protein imaging in P. falciparum; liver-stage expression by immunofluorescence

    PMID:7957747 PMID:8050527 PMID:8058359

    Open questions at the time
    • Functional consequence of domain segregation not tested
    • Relationship between EXP1 and EXP-2 not mechanistically defined
  4. 1996 Low

    Cross-species orthology (PyHEP17, P. berghei antigen) and antisense/immunization phenotypes provided the first functional evidence that EXP1 matters for parasite survival and protective immunity.

    Evidence Ortholog cloning, cross-reactive antibodies, mouse immunization/protection, and antisense oligonucleotide inhibition in P. yoelii, P. berghei and P. falciparum

    PMID:8663412 PMID:8825207

    Open questions at the time
    • Antisense phenotype is indirect with limited mechanistic resolution
    • Molecular basis of essentiality not identified
  5. 2002 High

    Showing the EXP1 signal sequence directs GFP chimeras to the PV by default and can redirect other proteins into the ER translocation pathway defined how EXP1 is trafficked and revealed subcompartmentation within the PV.

    Evidence GFP-chimera transfection with FRAP and dual lipid labeling, and cell-free translocation of chimeric constructs in P. falciparum

    PMID:10645548 PMID:12456681

    Open questions at the time
    • In vivo trafficking route to PVM not yet distinguished from other pathways
    • Determinants of PV subcompartmentation unknown
  6. 2006 Medium

    Demonstrating that EXP1 forms oligomeric arrays occupying microdomains distinct from ETRAMP arrays established that the PVM is organized into segregated protein assemblies rather than a homogeneous membrane.

    Evidence In vivo chemical cross-linking, recombinant expression in bacterial membranes, and immunofluorescence in P. falciparum; earlier charge-based domain comparison

    PMID:11566306 PMID:12686607 PMID:12868595 PMID:16420351

    Open questions at the time
    • Functional role of EXP1 oligomers not defined
    • Composition of EXP1 microdomains not resolved
  7. 2014 Medium

    Assigning EXP1 a membrane glutathione S-transferase activity that degrades hematin and is inhibited by artesunate proposed an enzymatic role linked to antimalarial drug action.

    Evidence Computational prediction, in vitro GST assay with hematin substrate, and artesunate inhibition/drug-pressure profiling in P. falciparum

    PMID:25126794

    Open questions at the time
    • In vitro enzymatic activity not shown to explain in vivo essentiality
    • Physiological relevance later challenged by conditional knockout
  8. 2017 High

    Mapping a C-terminal EXP1 interaction with host Apolipoprotein H, and showing PVM trafficking is PTEX-independent, defined a liver-stage host-interaction function and separated EXP1 delivery from the canonical protein-export route.

    Evidence Interaction mapping, C-terminal truncation mutants, ApoH siRNA knockdown and in vivo sporozoite challenge in P. berghei; misfolded-construct and conditional PTEX-inactivation trafficking in P. falciparum; liver-stage trafficking block by torins

    PMID:23836641 PMID:27892646 PMID:28137845

    Open questions at the time
    • Molecular consequence of ApoH binding for parasite development not fully defined
    • Trafficking machinery that delivers EXP1 to the PVM not identified
  9. 2018 Medium

    Localizing EXP1 to dense granules pre-invasion and validating it as a PVM BioID anchor clarified its delivery route and enabled proteomic mapping of the PVM neighborhood.

    Evidence IFA/immunoEM co-localization with RESA in P. falciparum merozoites; BioID proximity labeling with EXP1-BirA* in P. berghei blood stages

    PMID:29404413 PMID:29886341

    Open questions at the time
    • Which BioID-identified proteins are direct EXP1 partners not determined
    • Mechanism of dense-granule-to-PVM translocation unresolved
  10. 2019 High

    Conditional genetics resolved the essential function: EXP1 is required for the correct localization and channel function of EXP2, hence for PVM nutrient uptake, and its essentiality is independent of the earlier-proposed GST activity; domain analysis separated blood-stage from mosquito/liver-stage requirements.

    Evidence DiCre conditional knockout with PVM patch-clamp and EXP2 localization, TetR-DOZI/CRISPR-Cpf1 conditional knockdown with BioID and ultrastructural EM in P. falciparum; CRISPR domain-truncation multi-stage phenotyping in P. berghei

    PMID:31364224 PMID:31568532 PMID:31990132

    Open questions at the time
    • Molecular mechanism by which EXP1 organizes EXP2 not defined
    • Whether EXP1 physically contacts EXP2 in the channel not established

Open questions

Synthesis pass · forward-looking unresolved questions
  • How EXP1 oligomers physically organize EXP2 into a functional nutrient-permeable channel, and what the structural basis of this interaction is, remain unresolved.
  • No structure of EXP1 or the EXP1/EXP2 assembly
  • Direct physical interaction with EXP2 not demonstrated
  • Mechanism linking EXP1 microdomains to channel function unknown

Mechanism profile

Synthesis pass · controlled-vocabulary classification
Partners
EXP-2 (CO-LOCALIZATION AT PVM) [#3]EXP2 (FUNCTIONAL/ORGANIZATIONAL DEPENDENCY; EXP1 REQUIRED FOR CORRECT EXP2 LOCALIZATION AND NUTRIENT-PERMEABLE CHANNEL ACTIVITY) [#17, #19]HOST APOLIPOPROTEIN H (APOH), BOUND VIA THE EXP1 C-TERMINAL DOMAIN IN LIVER STAGE [#12]
Complex memberships
EXP1 oligomeric PVM microdomain arrays (distinct from ETRAMP arrays) [#9]

Evidence

Reading pass · 25 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1987 EXP1 (exp-1) is exported from P. falciparum parasites into a new compartment within the host erythrocyte; the gene contains two introns and is highly conserved across parasite lines, suggesting an important function. Monoclonal antibody localization, gene cloning and sequencing The EMBO journal Medium 2438130
1985 EXP1 is a ~23 kDa blood-stage protein with a signal peptide and an internal hydrophobic transmembrane anchor sequence; it shares antigenic determinants with sporozoites due to tetrapeptide repeats related to the circumsporozoite protein. cDNA cloning, nucleotide sequencing, affinity-purified antibody immunoassay Proceedings of the National Academy of Sciences of the United States of America Medium 2410913
1991 EXP1 is an integral membrane protein: in a cell-free translation-translocation system it was inserted into canine pancreatic microsomes with its N-terminus protected from proteinase K (facing the lumen) and its C-terminus exposed. In vivo, EXP1 is alkali-resistant (membrane-integrated) and segment-specific antibodies confirm the N-terminus faces the vesicle interior while the C-terminus is protease-accessible, consistent with a single-pass topology. Cell-free translation/translocation into microsomes, proteinase K protection assay, alkaline extraction, segment-specific monoclonal antibodies Molecular and biochemical parasitology High 1852170
1994 EXP1 is located at the parasitophorous vacuole membrane (PVM) and in membrane-bound compartments in the erythrocyte cytoplasm; a second exported protein (EXP-2, 35 kDa) co-localizes with EXP1 at these sites. Monoclonal antibody co-localization, membrane fractionation, detergent solubilization, alkali extraction Parasitology Medium 8058359
1994 EXP1 concentrates in membrane domains on the periphery of the parasite and in the tubovesicular membrane network (TVN), as shown by simultaneous lipid and protein fluorescence imaging; its distribution is distinct from a 45 kDa Maurer's cleft protein, indicating domain segregation within the TVN. High-resolution confocal microscopy with fluorescent sphingolipid labeling and immunostaining Experimental parasitology Medium 7957747
2002 The N-terminal signal sequence of EXP1, when fused to GFP, directs the chimeric protein to the parasitophorous vacuole (default secretory destination) in transfected parasites; some chimeric protein is redirected to the food vacuole. FRAP studies revealed that the PV contains subcompartments that are only partially interconnected. Transfection of GFP chimeras, live fluorescence microscopy, photobleaching (FRAP), dual lipid labeling The Journal of biological chemistry High 12456681
2003 EXP1 and ETRAMP family proteins are both PVM-resident, but ETRAMPs (positively charged) and EXP1 (negatively charged integral PVM protein) define separate PVM domains, suggesting functionally distinct microdomains with oppositely charged surface coats. Stage-specific expression of ETRAMPs coincides with morphological changes in development. Northern and Western blotting, colocalization by fluorescence microscopy, selective permeabilization, immunoelectron microscopy Molecular biology of the cell Medium 12686607
2003 EXP1 is a component of a continuous membrane network of parasite origin in the erythrocyte cytoplasm (comprising TVM, Maurer's clefts, and membrane whorls), as shown by co-localization at light and electron microscopy levels; small vesicles (15–25 nm) were observed at sites where this network contacts the erythrocyte plasma membrane. Immunofluorescence and immunoelectron microscopy, vital staining with LysoSensor Green European journal of cell biology Medium 12868595
2001 EXP1 (PfEXP1), together with internalized host membrane proteins, can be detected in detergent-resistant membrane (DRM) raft fractions within the parasitophorous vacuole, indicating that lipid rafts are present at the PVM. Detergent-resistant membrane (DRM) fractionation, Western blotting International journal for parasitology Low 11566306
2006 In vivo cross-linking in asexual P. falciparum stages revealed that EXP1 and ETRAMP family members form oligomeric arrays in the PVM; each ETRAMP and EXP1 define separate, non-overlapping arrays (microdomains). Recombinant ETRAMPs oligomerize independently in bacterial membranes, but EXP1 arrays are distinct from ETRAMP arrays. In vivo chemical cross-linking, recombinant protein expression in bacterial membranes, immunofluorescence microscopy Molecular microbiology Medium 16420351
2014 EXP1 functions as a membrane glutathione S-transferase (mGST): it efficiently degrades cytotoxic hematin in vitro and is potently inhibited by artesunate (nanomolar potency). EXP1 is associated with artesunate metabolism and susceptibility in drug-pressured parasites, implicating it in the mode of action of artesunate. Computational network analysis (supergenomic compression) for prediction; in vitro GST activity assay with hematin substrate; artesunate inhibition assay; drug-pressured parasite metabolic profiling Cell Medium 25126794
2013 EXP1 is a dynamic PVM protein during liver-stage infection; torins block trafficking of EXP1 to the liver-stage PVM, leading to parasite elimination by the hepatocyte. This effect is specific to liver stage and distinct from blood-stage action. Immunofluorescence microscopy of liver-stage parasites treated with torins, in vitro and in vivo parasite viability assays Proceedings of the National Academy of Sciences of the United States of America Medium 23836641
2017 The C-terminal region of EXP1 binds host Apolipoprotein H (ApoH) during hepatic Plasmodium development. Expression of a C-terminally truncated EXP1 missing the ApoH-interaction site, or siRNA knockdown of ApoH in hepatic cells or mouse livers, impairs intrahepatic parasite development. Infection of mice with sporozoites expressing truncated EXP1 reduces liver burden and delays blood-stage patency. Protein interaction mapping, truncation mutants, RNA interference (siRNA) knockdown of ApoH in cells and mice, in vivo sporozoite challenge with mutant parasites Proceedings of the National Academy of Sciences of the United States of America High 28137845
2017 Trafficking of EXP1 to the PVM is independent of the folding state of the protein and continues unabated upon inactivation of the PTEX translocon, indicating that PVM membrane protein trafficking occurs by a mechanism distinct from PTEX-mediated protein export. Transfection with misfolded EXP1 constructs, conditional PTEX inactivation, fluorescence microscopy to track PVM localization Cellular microbiology Medium 27892646
2017 EXP1 recombinant protein shows potent in vitro inhibition of membrane glutathione S-transferase activity by chloroquine (IC50 ~9 nM with hematin substrate; ~19 nM with CDNB), suggesting chloroquine may inhibit EXP1 mGST activity without requiring iron-dependent activation. In vitro GST activity assay with recombinant EXP1, hematin and CDNB substrates, chloroquine inhibition dose-response International journal for parasitology. Drugs and drug resistance Low 29324251
2018 EXP1 is initially localized to dense granules in P. falciparum merozoites (co-localizing with RESA) and is translocated to the PVM after erythrocyte invasion, as confirmed by immunofluorescence and immunoelectron microscopy. Immunofluorescence assay (IFA) with anti-EXP1 and anti-RESA antibodies, immunoelectron microscopy Parasitology international Medium 29886341
2018 BioID proximity labeling using EXP1 fused to BirA* in P. berghei blood-stage parasites identified 61 known and candidate PVM proteins, validating EXP1 as a PVM resident suitable as a BioID anchor and expanding the PVM proteome. BioID (proximity biotinylation with BirA* fused to EXP1), affinity purification, LC-MS/MS, label-free quantitation mSphere Medium 29404413
2019 EXP1 is essential for P. falciparum intraerythrocytic survival. Conditional knockout of EXP1 abolishes the nutrient-permeable channel activity at the PVM (measured by patch-clamp) and disrupts the correct localization of EXP2 (a pore-forming protein required for nutrient-permeable channel and protein export). Loss of EXP1 impairs only the nutrient-permeable channel activity, not protein export via PTEX. Parasites with reduced EXP1 become hypersensitive to low nutrient conditions, confirming EXP1 is specifically required for functional expression of EXP2 as a nutrient-permeable channel. Conditional knockout (DiCre-based), patch-clamp electrophysiology of PVM, immunofluorescence microscopy of EXP2 localization, nutrient deprivation survival assay PLoS biology High 31568532
2019 The GST activity previously attributed to EXP1 cannot account for its essential function in vivo, as conditional knockdown recapitulated the essential phenotype independently of any GST activity. Conditional knockdown (TetR-DOZI-aptamer system), intraerythrocytic growth assays Cellular microbiology Medium 31990132
2020 EXP1 is required for proper organization of EXP2 within the PVM. EXP1 knockdown causes profound changes in vacuole ultrastructure (increased PVM–parasite plasma membrane separation, abnormal membrane structures) and substantially alters EXP2 distribution but does not affect HSP101 (unfoldase) distribution or PTEX translocon activity. CRISPR/Cpf1-based installation of TetR-DOZI-aptamer conditional knockdown, BioID2 proximity labeling at PVM, immunofluorescence and ultrastructural electron microscopy Cellular microbiology High 31990132
2019 In P. berghei, the N-terminal domain of EXP1 is essential for parasite blood-stage survival, while the C-terminal (CT) domain is required for normal mosquito-stage development and for correct EXP1 localization to the PVM in intrahepatic parasites; truncation of the CT domain severely limits hepatic replication and prevents egress into the blood. CRISPR-based truncation mutants of PbEXP1, mouse infection models, immunofluorescence microscopy Cellular microbiology High 31364224
1999 The signal sequence of EXP1, when fused to PfHRPI, diverts HRPI away from the microsomal translocation machinery, demonstrating that the EXP1 signal sequence actively engages the ER translocation pathway and can redirect other proteins to it. Cell-free translation-translocation assay with chimeric constructs in pancreatic microsomes Novartis Foundation symposium Medium 10645548
1994 EXP1 protein is expressed in P. falciparum liver-stage parasites, not only blood stages, as demonstrated by immunofluorescence staining of infected hepatocytes. Immunofluorescence assay of infected hepatocytes Experimental parasitology Low 8050527
1996 The P. yoelii ortholog of EXP1 (PyHEP17) shares 37% amino acid identity with PfEXP1, has a similar expression pattern in hepatocytes and erythrocytes, and shows antigenic cross-reactivity; immunization with PyHEP17 induces protective antibodies and CTLs in mice, establishing the P. falciparum EXP1 as the functional homolog. Gene cloning and sequencing, immunological cross-reactivity assays, mouse immunization and protection studies The Journal of biological chemistry Medium 8663412
1996 A 43 kDa P. berghei antigen sharing immunological cross-reactivity with PfEXP1 was identified at the parasite surface; antisense phosphorothioate oligodeoxynucleotides targeting exp-1 mRNA inhibited P. falciparum development in vitro by 47% and extended lifespan of P. berghei-infected mice by 2–4-fold, suggesting EXP1 is functionally important for parasite survival. Cross-reactive antibody localization, antisense oligodeoxynucleotide inhibition in vitro and in vivo mouse experiments Parasitology research Low 8825207

Source papers

Stage 0 corpus · 69 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2003 etramps, a new Plasmodium falciparum gene family coding for developmentally regulated and highly charged membrane proteins located at the parasite-host cell interface. Molecular biology of the cell 141 12686607
1987 A malaria protein exported into a new compartment within the host erythrocyte. The EMBO journal 135 2438130
2000 HLA-DR-promiscuous T cell epitopes from Plasmodium falciparum pre-erythrocytic-stage antigens restricted by multiple HLA class II alleles. Journal of immunology (Baltimore, Md. : 1950) 121 10878392
1991 An exported protein of Plasmodium falciparum is synthesized as an integral membrane protein. Molecular and biochemical parasitology 107 1852170
2002 The signal sequence of exported protein-1 directs the green fluorescent protein to the parasitophorous vacuole of transfected malaria parasites. The Journal of biological chemistry 100 12456681
1990 Genetic diversity of Plasmodium falciparum shows geographical variation. The American journal of tropical medicine and hygiene 98 2187364
2014 Supergenomic network compression and the discovery of EXP1 as a glutathione transferase inhibited by artesunate. Cell 93 25126794
1991 Population genetics of Plasmodium falciparum within a malaria hyperendemic area. Parasitology 88 1719468
1985 A blood stage antigen of Plasmodium falciparum shares determinants with the sporozoite coat protein. Proceedings of the National Academy of Sciences of the United States of America 86 2410913
2013 Spatial association with PTEX complexes defines regions for effector export into Plasmodium falciparum-infected erythrocytes. Nature communications 75 23361006
1996 Identification and characterization of the protective hepatocyte erythrocyte protein 17 kDa gene of Plasmodium yoelii, homolog of Plasmodium falciparum exported protein 1. The Journal of biological chemistry 72 8663412
2003 Evidence for trafficking of PfEMP1 to the surface of P. falciparum-infected erythrocytes via a complex membrane network. European journal of cell biology 69 12868595
2013 Torins are potent antimalarials that block replenishment of Plasmodium liver stage parasitophorous vacuole membrane proteins. Proceedings of the National Academy of Sciences of the United States of America 68 23836641
2006 Organization of ETRAMPs and EXP-1 at the parasite-host cell interface of malaria parasites. Molecular microbiology 64 16420351
2019 EXP1 is critical for nutrient uptake across the parasitophorous vacuole membrane of malaria parasites. PLoS biology 61 31568532
1992 Longitudinal study of Plasmodium falciparum polymorphic antigens in a malaria-endemic population. Infection and immunity 61 1371764
1998 Simultaneous induction of multiple antigen-specific cytotoxic T lymphocytes in nonhuman primates by immunization with a mixture of four Plasmodium falciparum DNA plasmids. Infection and immunity 59 9712767
2004 Natural antibody response to Plasmodium falciparum Exp-1, MSP-3 and GLURP long synthetic peptides and association with protection. Parasite immunology 58 15541030
2014 Profiling the humoral immune responses to Plasmodium vivax infection and identification of candidate immunogenic rhoptry-associated membrane antigen (RAMA). Journal of proteomics 53 24607491
1994 Characterization of membrane proteins exported from Plasmodium falciparum into the host erythrocyte. Parasitology 53 8058359
1994 Plasmodium falciparum: protein localization along a novel, lipid-rich tubovesicular membrane network in infected erythrocytes. Experimental parasitology 50 7957747
2020 EXP1 is required for organisation of EXP2 in the intraerythrocytic malaria parasite vacuole. Cellular microbiology 47 31990132
2001 Transport mechanisms in Plasmodium-infected erythrocytes: lipid rafts and a tubovesicular network. International journal for parasitology 47 11566306
2000 Cytotoxic T-lymphocyte epitopes for HLA-B53 and other HLA types in the malaria vaccine candidate liver-stage antigen 3. Infection and immunity 44 10603392
2011 Measuring naturally acquired immune responses to candidate malaria vaccine antigens in Ghanaian adults. Malaria journal 39 21689436
2017 Plasmodium berghei EXP-1 interacts with host Apolipoprotein H during Plasmodium liver-stage development. Proceedings of the National Academy of Sciences of the United States of America 38 28137845
1994 Plasmodium falciparum: exported protein-1, a blood stage antigen, is expressed in liver stage parasites. Experimental parasitology 34 8050527
2018 BioID Reveals Novel Proteins of the Plasmodium Parasitophorous Vacuole Membrane. mSphere 33 29404413
2012 Clinical trial in healthy malaria-naïve adults to evaluate the safety, tolerability, immunogenicity and efficacy of MuStDO5, a five-gene, sporozoite/hepatic stage Plasmodium falciparum DNA vaccine combined with escalating dose human GM-CSF DNA. Human vaccines & immunotherapeutics 33 23151451
1991 Genetic evidence for the importance of interrupted feeding by mosquitoes in the transmission of malaria. Transactions of the Royal Society of Tropical Medicine and Hygiene 32 1755049
2004 Effect on antibody and T-cell responses of mixing five GMP-produced DNA plasmids and administration with plasmid expressing GM-CSF. Genes and immunity 31 15318164
1998 In vitro expression and in vivo immunogenicity of Plasmodium falciparum pre-erythrocytic stage DNA vaccines. International journal of molecular medicine 31 9854139
2022 Multi-Dose Priming Regimens of PfSPZ Vaccine: Safety and Efficacy against Controlled Human Malaria Infection in Equatoguinean Adults. The American journal of tropical medicine and hygiene 27 35130487
2019 The Candidate Blood-stage Malaria Vaccine P27A Induces a Robust Humoral Response in a Fast Track to the Field Phase 1 Trial in Exposed and Nonexposed Volunteers. Clinical infectious diseases : an official publication of the Infectious Diseases Society of America 24 29945169
2007 SELDI-TOF-MS analysis of chloroquine resistant and sensitive Plasmodium falciparum strains. Proteomics 24 17295353
2005 HLA-A2 supertype-restricted cell-mediated immunity by peripheral blood mononuclear cells derived from Malian children with severe or uncomplicated Plasmodium falciparum malaria and healthy controls. Infection and immunity 24 16113298
2015 Salmonella flagellin is a potent carrier-adjuvant for peptide conjugate to induce peptide-specific antibody response in mice. Vaccine 21 25765964
2018 Fitness Loss under Amino Acid Starvation in Artemisinin-Resistant Plasmodium falciparum Isolates from Cambodia. Scientific reports 20 30135481
2014 The subcellular location of ovalbumin in Plasmodium berghei blood stages influences the magnitude of T-cell responses. Infection and immunity 18 25156724
1991 A Plasmodium falciparum malaria vaccine candidate which contains epitopes from the circumsporozoite protein and a blood stage antigen, 5.1. Molecular and biochemical parasitology 17 1719416
2018 Plasmodium falciparum Exported Protein 1 is localized to dense granules in merozoites. Parasitology international 15 29886341
2007 Characterization of Maurer's clefts in Plasmodium falciparum-infected erythrocytes. The American journal of tropical medicine and hygiene 15 17255224
2003 ELISA detection of vivax malaria with recombinant multiple stage-specific antigens and its application to survey of residents in endemic areas. The Korean journal of parasitology 14 14699261
1989 Immune response to a synthetic peptide corresponding to an epitope of a parasitophorous vacuole membrane antigen from Plasmodium falciparum. Journal of immunology (Baltimore, Md. : 1950) 14 2473129
2002 Recognition of synthetic polypeptides corresponding to the N- and C-terminal fragments of Plasmodium falciparum Exp-1 by T-cells and plasma from human donors from African endemic areas. Parasite immunology 13 11982859
2021 HIV infection and placental malaria reduce maternal transfer of multiple antimalarial antibodies in Mozambican women. The Journal of infection 12 33636218
2022 Evaluation of antibody serology to determine current helminth and Plasmodium falciparum infections in a co-endemic area in Southern Mozambique. PLoS neglected tropical diseases 10 35727821
2017 Trafficking of PfExp1 to the parasitophorous vacuolar membrane of Plasmodium falciparum is independent of protein folding and the PTEX translocon. Cellular microbiology 10 27892646
2015 Protein profiling of mefloquine resistant Plasmodium falciparum using mass spectrometry-based proteomics. International journal of mass spectrometry 10 26869851
2001 Western blot diagnosis of vivax malaria with multiple stage-specific antigens of the parasite. The Korean journal of parasitology 9 11441504
1999 The transport of the histidine-rich protein I from Plasmodium falciparum is insensitive to brefeldin A. Novartis Foundation symposium 9 10645548
2020 Detection of EXP1-Specific CD4+ T Cell Responses Directed Against a Broad Range of Epitopes Including Two Promiscuous MHC Class II Binders During Acute Plasmodium falciparum Malaria. Frontiers in immunology 8 32038611
2016 Neutralizing Antibodies against Plasmodium falciparum Associated with Successful Cure after Drug Therapy. PloS one 8 27427762
2003 Humoral responses to defined malaria antigens in children living since birth under insecticide treated curtains in Burkina Faso. Acta tropica 8 12943972
1995 Mapping of a human T-lymphotropic virus type I gag protein epitope that cross-reacts with anti-Plasmodium falciparum antibodies. Journal of medical virology 8 7545215
1993 Mice immunized with a synthetic peptide construct corresponding to an epitope present on a Plasmodium falciparum antigen are protected against Plasmodium chabaudi challenge. Parasite immunology 8 7533280
2022 Deciphering the Plasmodium falciparum malaria-specific CD4+ T-cell response: ex vivo detection of high frequencies of PD-1+TIGIT+ EXP1-specific CD4+ T cells using a novel HLA-DR11-restricted MHC class II tetramer. Clinical and experimental immunology 7 35020841
2015 Characterization of Plasmodium vivax Early Transcribed Membrane Protein 11.2 and Exported Protein 1. PloS one 7 26011536
2017 Potential role of Plasmodium falciparum exported protein 1 in the chloroquine mode of action. International journal for parasitology. Drugs and drug resistance 6 29324251
2022 An Attenuated HSV-1-Derived Malaria Vaccine Expressing Liver-Stage Exported Proteins Induces Sterilizing Protection against Infectious Sporozoite Challenge. Vaccines 4 35214758
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
2019 A crucial role for the C-terminal domain of exported protein 1 during the mosquito and hepatic stages of the Plasmodium berghei life cycle. Cellular microbiology 4 31364224
2016 Intranasal immunization with a peptide conjugated to Salmonella flagellin induces both systemic and mucosal peptide-specific antibody responses in mice. Microbiology and immunology 4 27301339
2007 Identification of minimal CD8+ and CD4+ T cell epitopes in the Plasmodium yoelii hepatocyte erythrocyte protein 17kDa. Molecular immunology 4 17303242
2022 Cyclic constrained immunoreactive peptides from crucial P. falciparum proteins: potential implications in malaria diagnostics. Translational research : the journal of laboratory and clinical medicine 3 35697275
1998 Immune response against the exp-1 protein of Plasmodium falciparum results in antibodies that cross-react with human T-cell lymphotropic virus type 1 proteins. Clinical and diagnostic laboratory immunology 3 9729542
1996 Identification of a Plasmodium berghei antigen sharing common features with P. falciparum and P. chabaudi parasitophorous-vacuole membrane antigens. Parasitology research 3 8825207
2001 [Cloning and sequence analysis of exp-1 gene of Plasmodium falciparum FCC1/HN]. Zhongguo ji sheng chong xue yu ji sheng chong bing za zhi = Chinese journal of parasitology & parasitic diseases 0 12572082