Affinage · Plasmodium

SERA5

PF3D7_0207600 · serine repeat antigen 5

Audit flag: identity unverified
Annotated
2026-09-07
65 papers in source corpus 21 papers cited in narrative 21 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

SERA5 (PF3D7_0207600) is an abundant parasitophorous-vacuole protein that is essential for the asexual erythrocytic cycle of P. falciparum, where it functions to regulate the kinetics and efficiency of merozoite egress from the host erythrocyte (PMID:12228245, PMID:17893128, PMID:28683142). It localises to the parasitophorous vacuole of trophozoite- and schizont-stage parasites (PMID:12244052, PMID:12228245) and possesses a central papain-like domain that is catalytically dead in its native form: the canonical active-site Cys is replaced by Ser596, no protease activity is detectable from native SERA5, and crystal structures reveal a pseudo-zymogen fold in which the prodomain occludes the active-site cleft and further residues (Asp594, Tyr735) restrict substrate access (PMID:19591843, PMID:32955133, PMID:25599609). The essential role of SERA5 is non-enzymatic and genetically separable from any catalytic activity, since a Ser596Ala knock-in has no phenotype while full-length structural integrity is required (PMID:25599609). SERA5 function depends on proteolytic maturation: it is cleaved by PfSUB1 (and DPAP3) discharged into the vacuole just before rupture in a Ca2+-dependent manner, and a processing-refractory mutant fails to complement the egress defect of a conditional SERA5 knockout, which produces premature host-cell rupture and merozoites trapped within residual membranes (PMID:18246061, PMID:23217145, PMID:28683142). Beyond egress, the processed P47 N-terminal fragment appears on the merozoite and sporozoite surface and recruits host vitronectin, blocking macrophage phagocytosis and implicating SERA5 in molecular camouflage against host immunity (PMID:17875342, PMID:29567995), and SERA5 is phosphorylated by PfCDPK1 in a Ca2+-dependent manner prior to egress (PMID:29716996). In the P. berghei rodent-malaria model the serine-type SERA orthologues localise to the parasitophorous vacuole but are individually and jointly dispensable for the life cycle (PMID:20039882).

Mechanistic history

Synthesis pass · year-by-year structured walk · 12 steps
  1. 2002 High

    Establishing whether SERA5 is required at all for blood-stage parasites: repeated failure to disrupt the gene, while flanking SERA-cluster genes were deletable, defined SERA5 as indispensable for the asexual erythrocytic cycle.

    Evidence Targeted gene disruption by homologous recombination across the SERA cluster

    PMID:12228245 PMID:17893128

    Open questions at the time
    • Refractoriness to deletion does not reveal which molecular function is essential
    • Does not distinguish an enzymatic from a structural/regulatory role
  2. 2002 Medium

    Localising SERA5 to define its site of action: it resides in the parasitophorous vacuole of trophozoite/schizont-stage parasites, placing it in the compartment where egress is executed.

    Evidence Indirect immunofluorescence microscopy with specific antibodies

    PMID:12228245 PMID:12244052

    Open questions at the time
    • IFA alone does not resolve sub-vacuolar distribution
    • Does not establish molecular partners in the vacuole
  3. 2003 Medium

    Testing whether the papain-like domain is a functional enzyme: a refolded recombinant domain showed inhibitor-sensitive chymotrypsin-like serine protease activity, initially framing SERA5 as an active protease despite the Cys-to-Ser596 substitution.

    Evidence Recombinant expression, refolding, in vitro protease assay with serine-protease inhibitor

    PMID:13679369

    Open questions at the time
    • Activity was from a refolded recombinant form, not native protein
    • Later contradicted by studies finding no activity from native Ser596-containing SERA5
  4. 2008 High

    Connecting SERA5 to the egress machinery: chemical-genetic inhibition showed SERA5 is processed by PfSUB1 and DPAP3 immediately before rupture, and blocking this processing correlated with a block in egress.

    Evidence Covalent protease-inhibitor library screen with immunoblot of SERA5 processing

    PMID:18246061 PMID:23217145

    Open questions at the time
    • Correlation of processing with egress did not prove processed SERA5 is functionally required
    • Cleavage sites and fate of fragments not fully defined here
  5. 2009 High

    Explaining the catalytic ambiguity structurally: the crystal structure showed Ser596 in the Cys position and an active-site architecture (Asp594, Tyr735 occlusion) incompatible with canonical cysteine-protease catalysis.

    Evidence X-ray crystallography of the central protease-like domain

    PMID:19591843 PMID:32955133

    Open questions at the time
    • Structure alone cannot exclude non-canonical or regulated activity
    • Does not address the essential in vivo function
  6. 2009 Medium

    Testing genetic essentiality of the family in a tractable in vivo model: P. berghei serine-type SERA orthologues localise to the PV but single and double knockouts complete the life cycle, showing these orthologues are non-vital in the rodent model.

    Evidence mCherry tagging, antibody localisation, and targeted gene replacement in P. berghei

    PMID:20039882

    Open questions at the time
    • Findings are in P. berghei orthologues, not PfSERA5 directly
    • Species divergence in essentiality left unexplained
  7. 2012 Medium

    Placing SERA5 processing within the Ca2+-triggered egress cascade: BAPTA-AM chelation blocked PfSUB1 discharge, preventing SERA5 processing and PVM rupture, positioning SERA5 cleavage downstream of a calcium signal.

    Evidence Time-lapse microscopy, Ca2+ chelation, PLC inhibition, immunoblot of SERA5 processing

    PMID:23217145

    Open questions at the time
    • Does not define the direct trigger for PfSUB1 discharge
    • Single-study chemical perturbations
  8. 2015 High

    Resolving whether SERA5's essential role is enzymatic: native and recombinant Ser596 SERA5 had no protease activity, a Ser596Ala knock-in was phenotypically silent, Ser596Cys restored recombinant activity, and the full-length protein could not be truncated/tagged — establishing an essential non-enzymatic, structurally intact role.

    Evidence In vitro activity assays, active-site mutagenesis, and multiple in-parasite genetic manipulations

    PMID:25599609

    Open questions at the time
    • Does not define the precise molecular action of the intact protein
    • Leaves the mechanism by which structural integrity is needed unresolved
  9. 2017 High

    Defining the physiological function directly: conditional deletion caused premature rupture and failure of merozoite dissemination; wild-type but not a processing-refractory mutant rescued, proving SERA5 regulates egress kinetics and requires SUB1-mediated processing.

    Evidence DiCre conditional knockout, complementation, processing-refractory mutant, live imaging, cysteine-protease inhibitor

    PMID:28683142

    Open questions at the time
    • Molecular target of processed SERA5 during egress not identified
    • Why the premature-rupture phenotype requires cysteine protease activity is unresolved
  10. 2018 Medium

    Identifying an immune-evasion function: the P47/SE36 fragment directly binds host vitronectin and co-localises with it on merozoite surfaces, and VTN binding blocked phagocytosis of SE36-coated beads, implicating SERA5 in molecular camouflage.

    Evidence Serum protein screening, direct binding, IFA co-localisation, THP-1 phagocytosis assay

    PMID:29567995

    Open questions at the time
    • Camouflage shown with coated beads, not live parasites
    • In vivo relevance to immune evasion untested
  11. 2018 Medium

    Linking SERA5 to calcium-dependent kinase signalling: PfCDPK1 physically associates with SERA5 and phosphorylates it Ca2+-dependently prior to egress, with kinase inhibition blocking both phosphorylation and egress.

    Evidence Reciprocal co-IP/co-sedimentation, MS, in vitro kinase assay, purfalcamine inhibition, egress assay

    PMID:29716996

    Open questions at the time
    • Phosphosites on SERA5 not mapped
    • The claimed enhancement of proteolytic activity conflicts with evidence that native SERA5 has no protease activity
  12. 2020 High

    Confirming the inactive state structurally: high-resolution structures of the isolated enzyme domain and the prodomain-bound pseudo-zymogen showed the prodomain occludes the catalytic cleft in the conventional reverse orientation, consistent with a maintained inactive zymogen-like state.

    Evidence X-ray crystallography at 1.2 Å (domain) and 2.2 Å (pseudo-zymogen)

    PMID:32955133

    Open questions at the time
    • Whether or how the prodomain is removed in vivo is not defined
    • Does not connect the zymogen state to the egress-regulatory function

Open questions

Synthesis pass · forward-looking unresolved questions
  • The precise molecular mechanism by which processed, catalytically inactive SERA5 restrains egress timing and organizes merozoite dissemination — and its direct binding target(s) within the vacuole — remains unresolved.
  • No direct downstream effector or substrate of processed SERA5 identified
  • Functional meaning of PfCDPK1 phosphorylation and prodomain removal for egress not established
  • Species divergence in essentiality (dispensable in P. berghei, essential in P. falciparum) unexplained

Mechanism profile

Synthesis pass · controlled-vocabulary classification
Partners
DPAP3 (PROCESSING PROTEASE)HOST VITRONECTIN (VTN)PFCDPK1 (KINASE, PHOSPHORYLATES SERA5)PFPTKL PSEUDOKINASE (SAM-DOMAIN INTERACTION)PFSUB1 (PROCESSING PROTEASE)

Evidence

Reading pass · 21 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2002 SERA5 (PF3D7_0207600) is essential for the asexual erythrocytic cycle of P. falciparum: repeated attempts to disrupt the SERA5 gene by homologous recombination failed, while genes at the periphery of the SERA cluster on chromosome 2 could be disrupted, indicating SERA5 is indispensable for blood-stage parasite maintenance. Targeted gene disruption by homologous recombination (loss-of-function genetics) The Journal of biological chemistry High 12228245 17893128
2002 SERA5 protein localises within the parasitophorous vacuole of trophozoite- and schizont-stage intraerythrocytic parasites, as demonstrated by indirect immunofluorescence microscopy with SERA5-specific antibodies. Indirect immunofluorescence microscopy with specific polyclonal antibodies The Journal of biological chemistry Medium 12228245 12244052
2003 The central papain-like enzyme domain of SERA5 possesses serine protease activity: a recombinant form processed substrates downstream of aromatic residues (chymotrypsin-like specificity), and this activity was abolished by the serine protease inhibitor 3,4-diisocoumarin. The canonical catalytic Cys of papain is replaced by Ser596 in SERA5. Recombinant protein expression, refolding, in vitro protease activity assay, inhibitor studies The Journal of biological chemistry Medium 13679369
2008 SERA5 is proteolytically processed by PfSUB1 (subtilisin-family serine protease) and DPAP3 (cysteine protease dipeptidyl peptidase 3) just prior to erythrocyte rupture; pharmacological inhibition of either PfSUB1 or DPAP3 blocked SERA5 processing and was correlated with a block in parasite egress. Chemical genetic screen with covalent protease inhibitor library; immunoblot analysis of SERA5 processing in inhibitor-treated schizonts Nature chemical biology High 18246061 23217145
2009 Crystal structure of the central protease-like domain of SERA5 was solved, revealing: (1) Ser596 occupies the position of the active-site Cys; (2) the active-site architecture is not conducive to canonical cysteine-protease substrate binding; (3) Asp594 restricts substrate access; (4) the S2 specificity pocket is occluded by Tyr735. These structural anomalies are consistent with impaired/absent protease activity. X-ray crystallography Journal of molecular biology High 19591843 32955133
2009 In P. berghei, the two serine-type SERA orthologues (PbSERA1 and PbSERA2) display differential expression during late merozoite formation and localise to the parasitophorous vacuole, as shown by antibody localisation and in vivo mCherry fluorescent tagging. Single and double gene knockouts of P. berghei serine-type SERAs progressed normally through the full parasite life cycle, indicating non-vital roles in vivo in this rodent malaria model. Fluorescent protein tagging (mCherry), antibody localisation, targeted gene replacement (KO) Cellular microbiology Medium 20039882
2012 Chelation of intracellular Ca2+ in P. falciparum schizonts with BAPTA-AM blocks discharge of PfSUB1 from merozoite exonemes into the parasitophorous vacuole, which in turn prevents proteolytic processing of SERA5 and blocks parasitophorous vacuolar membrane (PVM) rupture and merozoite egress. Time-lapse video microscopy, intracellular Ca2+ chelation (BAPTA-AM), phospholipase C inhibition, immunoblot of SERA5 processing Cellular microbiology Medium 23217145
2013 SERA5 is present on the surface of sporozoites as well as merozoites: the processed 47 kDa N-terminal fragment (P47) was detected in sporozoites by Western blotting for the first time, using monoclonal antibodies raised against SERA5 N-terminal peptide FB-23. Western blotting, indirect immunofluorescence assay with monoclonal antibodies Peptides Medium 17875342
2013 SERA5 (P47 fragment) and SERA4 are shed from the merozoite surface at the tight junction during erythrocyte invasion, as demonstrated by real-time imaging and processing assays during live invasion events. Sequential immunoblot analysis and real-time live imaging of merozoite invasion Infection and immunity Medium 24218484
2015 SERA5 plays an indispensable non-enzymatic role in the P. falciparum asexual blood-stage life cycle: (1) no proteolytic activity was detected from parasite-derived or recombinant Ser596-containing SERA5; (2) substitution of Ser596 with Ala by targeted homologous recombination had no phenotypic consequence; (3) substitution of Ser596 with Cys yielded an active recombinant cysteine protease, showing the domain can bind peptide substrate but the native Ser cannot catalyse cleavage; (4) SERA5 could not be truncated or C-terminally tagged, establishing structural integrity of the full-length protein as essential. In vitro protease activity assay, site-directed mutagenesis of recombinant protein, targeted homologous recombination (Ser596Ala, Ser596Arg knock-in, internal tag insertion, C-terminal tag), parasite phenotyping Molecular microbiology High 25599609
2017 Conditional DiCre-mediated disruption of the SERA5 gene caused premature host cell rupture and failure of daughter merozoites to efficiently disseminate (retained within residual bounding membranes), demonstrating that SERA5 is a regulator of egress kinetics and efficiency. Complementation with wild-type SERA5 reversed the defect, whereas a processing-refractory SERA5 mutant failed to rescue, proving that SUB1-mediated proteolytic processing of SERA5 is required for its function. SERA5 was not required for poration or vesiculation of the host cell membrane, but the premature rupture phenotype required cysteine protease activity. Conditional DiCre gene deletion, genetic complementation, processing-refractory mutant expression, live imaging, invasion assay, cysteine protease inhibitor treatment PLoS pathogens High 28683142
2018 Vitronectin (VTN) from host serum directly binds to a 20-residue region in the C-terminal portion of the P47/SE36 N-terminal domain of SERA5; VTN co-localises with SERA5 P47 on schizont and merozoite surfaces; VTN bound to SE36 prevented phagocytosis of SE36-coated beads by THP-1 macrophages, suggesting SERA5 mediates molecular camouflage of merozoites against host immunity. Serum protein screening, direct binding assay, co-localisation (IFA), phagocytosis assay with THP-1 cells Scientific reports Medium 29567995
2018 SERA5 is phosphorylated prior to merozoite egress; calcium-dependent protein kinase 1 (PfCDPK1) physically associates with SERA5 (co-immunoprecipitation, co-sedimentation, co-immunolocalisation) and phosphorylates SERA5 in vitro in a Ca2+-dependent manner, enhancing its proteolytic activity; the PfCDPK1 inhibitor purfalcamine blocked SERA5 phosphorylation and activation both in vitro and in schizonts, blocking egress. Immunoprecipitation + MS identification of PfCDPK1, co-sedimentation, co-immunoprecipitation, co-immunolocalisation, in vitro kinase assay, kinase inhibitor (purfalcamine) treatment, egress assay The Journal of biological chemistry Medium 29716996
2019 SERA5 physically interacts with the pseudokinase PfpTKL via its SAM motif: recombinant PfpTKL SAM domain pulled down SERA5 from P. falciparum lysate, establishing SERA5 as a binding partner of this scaffolding pseudokinase in the parasitophorous vacuole context. Pulldown / co-immunoprecipitation of native parasite lysate with recombinant domain Scientific reports Low 31148576
2020 The crystal structure of the SERA5 pseudo-zymogen (enzyme domain plus cognate prodomain, PfSERA5PE) was solved to 2.2 Å resolution, and the isolated enzyme domain (PfSERA5E) was refined to 1.2 Å. The prodomain occludes the archetypal papain-like catalytic triad cleft in the same reverse orientation as conventional prodomains, consistent with SERA5 being maintained in an inactive zymogen-like state. X-ray crystallography (1.2 Å and 2.2 Å resolution structures) Protein science : a publication of the Protein Society High 32955133
2007 Deletion of SERA4 in P. falciparum resulted in a twofold compensatory increase in SERA5 mRNA levels, providing functional genetic evidence that SERA5 expression is regulated in response to loss of a related serine-type family member and is consistent with partial functional redundancy between SERA4 and SERA5. Gene knockout by homologous recombination, quantitative RT-PCR of SERA5 mRNA in SERA4-null parasites Infection and immunity Medium 17893128
2008 A 14-residue disulfide-bonded cyclic peptide (SBP1) identified by phage display against the SERA5 enzyme domain crosses both the erythrocyte and parasitophorous vacuole membranes and accumulates within the PV; treatment of parasite cultures with SBP1 compromised late-stage parasite development; SBP1 and SERA5 were also detected in the parasite cytosol, indicating parasite plasma membrane compromise, implicating the SERA5 enzyme domain in regulation of intraerythrocytic development. Phage display peptide selection, biochemical binding characterisation, parasite growth inhibition assay, immunolocalisation of peptide and SERA5 Infection and immunity Medium 18591232
2014 Protective epitopes of SERA5 recognised by inhibitory antibodies from naturally immune Ugandan adults reside in the intrinsically disordered N-terminal octamer-repeat and serine-rich regions; affinity-purified antibodies against these regions displayed high antibody-dependent cellular inhibition (ADCI) activity; spectroscopic and computational analysis confirmed these N-terminal regions are structurally unstructured. Synthetic peptide epitope mapping, affinity purification of antibodies, ADCI assay, structural analysis (spectroscopy + structure prediction) PloS one Medium 24886718
2012 Peptides derived from the C-terminal ~6 kDa region of the SERA5 active domain inhibit the recombinant SERA5 enzyme activity and delay parasite development in culture; molecular docking showed these peptides interact with the active site; the peptides co-localise with SERA5 in the parasite but do not affect SERA5 processing, indicating they act by direct active-site engagement. Synthetic peptide synthesis, in vitro enzyme inhibition assay, parasite growth/development assay, co-localisation (IFA), molecular docking Biochimica et biophysica acta Low 24769454
2012 The SERA5 prodomain (21.9 kDa N-terminal subdomain of the 50.8 kDa central domain) inhibits parasite development when added exogenously to parasite cultures at nanomolar concentrations, causing a significant delay in schizont-to-ring transition; a heptapeptide from its C-terminus (DNSDNMF) shows the same effect at ~1000-fold higher concentration and interacts with the catalytic domain, suggesting the prodomain regulates SERA5 activity. Recombinant prodomain production (E. coli), parasite culture growth inhibition assay, peptide interaction assay PloS one Low 22291957
2011 The structure of the P. berghei ICP C-terminal inhibitory domain in complex with falcipain-2 shows that the active-site architecture of SERA5 (serine-repeat antigen 5) is incompatible with ICP binding, explaining why the SERA5 protease-like domain is not a target for ICP-class cysteine protease inhibitors. X-ray crystallography (2.6 Å) of PbICP-C/falcipain-2 complex with structural inference about SERA5 Structure (London, England : 1993) Medium 21742259

Source papers

Stage 0 corpus · 65 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2004 Cysteine proteases of malaria parasites. International journal for parasitology 262 15582526
2008 Identification of proteases that regulate erythrocyte rupture by the malaria parasite Plasmodium falciparum. Nature chemical biology 202 18246061
2013 Robust inducible Cre recombinase activity in the human malaria parasite Plasmodium falciparum enables efficient gene deletion within a single asexual erythrocytic growth cycle. Molecular microbiology 171 23489321
2002 A subset of Plasmodium falciparum SERA genes are expressed and appear to play an important role in the erythrocytic cycle. The Journal of biological chemistry 137 12228245
2011 Falcipains and other cysteine proteases of malaria parasites. Advances in experimental medicine and biology 116 21660657
2015 Recent advances in recombinant protein-based malaria vaccines. Vaccine 92 26458807
2002 Serine repeat antigen (SERA5) is predominantly expressed among the SERA multigene family of Plasmodium falciparum, and the acquired antibody titers correlate with serum inhibition of the parasite growth. The Journal of biological chemistry 83 12244052
2003 Enzymic, phylogenetic, and structural characterization of the unusual papain-like protease domain of Plasmodium falciparum SERA5. The Journal of biological chemistry 77 13679369
2017 The Plasmodium falciparum pseudoprotease SERA5 regulates the kinetics and efficiency of malaria parasite egress from host erythrocytes. PLoS pathogens 73 28683142
2007 Evidence for a common role for the serine-type Plasmodium falciparum serine repeat antigen proteases: implications for vaccine and drug design. Infection and immunity 66 17893128
2012 Proteolytic activation of the essential parasitophorous vacuole cysteine protease SERA6 accompanies malaria parasite egress from its host erythrocyte. The Journal of biological chemistry 62 22984267
2013 Sequential processing of merozoite surface proteins during and after erythrocyte invasion by Plasmodium falciparum. Infection and immunity 60 24218484
2013 Phase 1b randomized trial and follow-up study in Uganda of the blood-stage malaria vaccine candidate BK-SE36. PloS one 59 23724021
2015 Plasmodium falciparum SERA5 plays a non-enzymatic role in the malarial asexual blood-stage lifecycle. Molecular microbiology 53 25599609
2010 Evidences of protection against blood-stage infection of Plasmodium falciparum by the novel protein vaccine SE36. Parasitology international 53 20493274
2006 High titers of IgG antibodies against Plasmodium falciparum serine repeat antigen 5 (SERA5) are associated with protection against severe malaria in Ugandan children. The American journal of tropical medicine and hygiene 53 16474069
2012 Ca(2+) -mediated exocytosis of subtilisin-like protease 1: a key step in egress of Plasmodium falciparum merozoites. Cellular microbiology 51 23217145
2013 TLR9 adjuvants enhance immunogenicity and protective efficacy of the SE36/AHG malaria vaccine in nonhuman primate models. Human vaccines & immunotherapeutics 38 23291928
2014 Protective epitopes of the Plasmodium falciparum SERA5 malaria vaccine reside in intrinsically unstructured N-terminal repetitive sequences. PloS one 36 24886718
2009 Structural insights into the protease-like antigen Plasmodium falciparum SERA5 and its noncanonical active-site serine. Journal of molecular biology 35 19591843
2009 The Plasmodium serine-type SERA proteases display distinct expression patterns and non-essential in vivo roles during life cycle progression of the malaria parasite. Cellular microbiology 35 20039882
2006 Comparative transcriptomal analysis of isogenic Plasmodium falciparum clones of distinct antigenic and adhesive phenotypes. Molecular and biochemical parasitology 35 17196675
2011 Plasmodium falciparum serine repeat antigen 5 (SE36) as a malaria vaccine candidate. Vaccine 33 21718740
2011 Structural basis for the regulation of cysteine-protease activity by a new class of protease inhibitors in Plasmodium. Structure (London, England : 1993) 31 21742259
2007 Phylogeny and evolution of the SERA multigene family in the genus Plasmodium. Journal of molecular evolution 31 17609844
2008 Deletion of the Plasmodium falciparum merozoite surface protein 7 gene impairs parasite invasion of erythrocytes. Eukaryotic cell 30 18820076
2012 Geographic differentiation of polymorphism in the Plasmodium falciparum malaria vaccine candidate gene SERA5. Vaccine 25 22230587
2018 Molecular Camouflage of Plasmodium falciparum Merozoites by Binding of Host Vitronectin to P47 Fragment of SERA5. Scientific reports 24 29567995
2018 Calcium-dependent phosphorylation of Plasmodium falciparum serine repeat antigen 5 triggers merozoite egress. The Journal of biological chemistry 23 29716996
2013 In Silico screening on the three-dimensional model of the Plasmodium vivax SUB1 protease leads to the validation of a novel anti-parasite compound. The Journal of biological chemistry 22 23653352
2020 First-in-human randomised trial and follow-up study of Plasmodium falciparum blood-stage malaria vaccine BK-SE36 with CpG-ODN(K3). Vaccine 21 33012605
2018 Associations between IgG reactivity to Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) antigens and Burkitt lymphoma in Ghana and Uganda case-control studies. EBioMedicine 20 30579868
2008 Inhibition of malaria parasite development by a cyclic peptide that targets the vital parasite protein SERA5. Infection and immunity 20 18591232
2020 Characteristic features of the SERA multigene family in the malaria parasite. Parasites & vectors 18 32252804
2007 Antibodies elicited by a virosomally formulated Plasmodium falciparum serine repeat antigen-5 derived peptide detect the processed 47 kDa fragment both in sporozoites and merozoites. Peptides 18 17875342
2004 The serine repeat antigen (SERA) gene family phylogeny in Plasmodium: the impact of GC content and reconciliation of gene and species trees. Molecular biology and evolution 18 15306658
2014 Synthetic peptides derived from the C-terminal 6kDa region of Plasmodium falciparum SERA5 inhibit the enzyme activity and malaria parasite development. Biochimica et biophysica acta 17 24769454
2016 Antibody titres and boosting after natural malaria infection in BK-SE36 vaccine responders during a follow-up study in Uganda. Scientific reports 16 27703240
2006 Pigmented monocytes are negative correlates of protection against severe and complicated malaria in Ugandan children. The American journal of tropical medicine and hygiene 16 16687669
2018 Plasmodium falciparum MSP3 Exists in a Complex on the Merozoite Surface and Generates Antibody Response during Natural Infection. Infection and immunity 15 29760216
2017 A novel Pfs38 protein complex on the surface of Plasmodium falciparum blood-stage merozoites. Malaria journal 14 28202027
2023 Safety and immunogenicity of BK-SE36/CpG malaria vaccine in healthy Burkinabe adults and children: a phase 1b randomised, controlled, double-blinded, age de-escalation trial. Frontiers in immunology 11 37908361
2021 Assessment of Mixed Plasmodium falciparum sera5 Infection in Endemic Burkitt Lymphoma: A Case-Control Study in Malawi. Cancers 11 33918470
2022 Safety and immunogenicity of BK-SE36 in a blinded, randomized, controlled, age de-escalating phase Ib clinical trial in Burkinabe children. Frontiers in immunology 9 36119062
2019 Plasmodium pseudo-Tyrosine Kinase-like binds PP1 and SERA5 and is exported to host erythrocytes. Scientific reports 9 31148576
2013 Association of naturally acquired IgG antibodies against Plasmodium falciparum serine repeat antigen-5 with reduced placental parasitemia and normal birth weight in pregnant Ugandan women: a pilot study. Parasitology international 9 23395684
2012 Inhibitory potential of prodomain of Plasmodium falciparum protease serine repeat antigen 5 for asexual blood stages of parasite. PloS one 9 22291957
2011 Antibodies reactive to Plasmodium falciparum serine repeat antigen in children with Burkitt lymphoma from Ghana. International journal of cancer 9 21630256
2023 Plasmodium falciparum infection coinciding with the malaria vaccine candidate BK-SE36 administration interferes with the immune responses in Burkinabe children. Frontiers in immunology 8 36993981
2017 Pooled-DNA sequencing identifies genomic regions of selection in Nigerian isolates of Plasmodium falciparum. Parasites & vectors 5 28662682
2008 [Malaria vaccine]. Nihon rinsho. Japanese journal of clinical medicine 5 18939502
2020 Structure of the Plasmodium falciparum PfSERA5 pseudo-zymogen. Protein science : a publication of the Protein Society 4 32955133
2020 Age-dependent carriage of alleles and haplotypes of Plasmodium falciparum sera5, eba-175, and csp in a region of intense malaria transmission in Uganda. Malaria journal 4 33032613
2016 Immunogenicity and protection from malaria infection in BK-SE36 vaccinated volunteers in Uganda is not influenced by HLA-DRB1 alleles. Parasitology international 4 27343834
2015 Plasmodium vivax: N-terminal diversity in the blood stage SERA genes from Indian isolates. Blood cells, molecules & diseases 3 25976464
2013 Plasmodium vivax: C-terminal diversity in the blood stage SERA genes from Indian field isolates. Experimental parasitology 3 23485360
2023 Immune tolerance caused by repeated P. falciparum infection against SE36 malaria vaccine candidate antigen and the resulting limited polymorphism. Parasitology international 2 38101534
2022 African-specific polymorphisms in Plasmodium falciparum serine repeat antigen 5 in Uganda and Burkina Faso clinical samples do not interfere with antibody response to BK-SE36 vaccination. Frontiers in cellular and infection microbiology 2 36590593
2018 Genetic Diversity in C-terminal of SERA5 Gene in the Blood Stage of Human Isolates of Plasmodium vivax in Sistan and Baluchistan, Iran. Iranian journal of parasitology 1 30483336
2016 In silico approach to ascertain the calcium dependent role of Plasmodium falciparum SERA5. Journal of biomolecular structure & dynamics 1 26725489
2026 Bioinformatic analysis of Plasmodium knowlesi Serine Repeat Antigen 3 (SERA3) sequences for antimalarial peptide development. Acta tropica 0 42431567
2025 Therapeutic Targeting and Role of Cysteine Proteases in the Life Cycle of Malaria Parasite. Current medicinal chemistry 0 39185645
2024 Plasmodium proteases and their role in development of Malaria vaccines. Advances in parasitology 0 39448193
2017 Safety, immunogenicity, and cross-species protection of a plasmid DNA encoding Plasmodium falciparum SERA5 polypeptide, microbial epitopes and chemokine genes in mice and olive baboons. Journal of biomedical research 0 28808204
2013 [Development and application of next generation SE36 malaria vaccine formulated with a novel adjuvant: approach to travelers' vaccine]. Yakugaku zasshi : Journal of the Pharmaceutical Society of Japan 0 24189556