Immunogenicity and antigenic properties of Pf332-C231, a fragment of a non-repeat region of the Plasmodium falciparum antigen Pf332

Balogun, Halima A.; Vasconcelos, Nina-Maria; Lindberg, R.; Haeggström, Malin; Moll, Kirsten; Chen, Q.; Wahlgren, Mats; Berzins, Klavs

doi:10.1016/j.vaccine.2009.09.110

Cited by 8 publications

(4 citation statements)

References 25 publications

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“…As a result, it is likely that antibodies towards the antigen are generated upon schizont rupture, at which time the protein is released into the extracellular environment. Previous studies using recombinant protein of the Pf332 regions EB200 and C231 (a C-terminally located region of Pf332, less rich in degenerate-repeats [47]), have reported that children lack antibodies against both parts of the molecule. However, antibodies were frequently found in older individuals, indicating a slow acquisition of Pf332 antibodies [14, 48].…”

Section: Discussionmentioning

confidence: 99%

Characterization of the Duffy-Binding-Like Domain ofPlasmodium falciparumBlood-Stage Antigen 332

Nilsson

Moll

Angeletti

et al. 2011

Malaria Research and Treatment

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Studies on Pf332, a major Plasmodium falciparum blood-stage antigen, have largely been hampered by the cross-reactive nature of antibodies generated against the molecule due to its high content of repeats, which are present in other malaria antigens. We previously reported the identification of a conserved domain in Pf332 with a high degree of similarity to the Duffy-binding-like (DBL) domains of the erythrocyte-binding-like (EBL) family. We here describe that antibodies towards Pf332-DBL are induced after repeated exposure to P. falciparum and that they are acquired early in life in areas of intense malaria transmission. Furthermore, a homology model of Pf332-DBL was found to be similar to the structure of the EBL-DBLs. Despite their similarities, antibodies towards Pf332-DBL did not display any cross-reactivity with EBL-proteins as demonstrated by immunofluorescence microscopy, Western blotting, and peptide microarray. Thus the DBL domain is an attractive region to use in further studies on the giant Pf332 molecule.

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Section: Discussionmentioning

confidence: 99%

Characterization of the Duffy-Binding-Like Domain ofPlasmodium falciparumBlood-Stage Antigen 332

Nilsson

Moll

Angeletti

et al. 2011

Malaria Research and Treatment

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“…The recognition of His-PfRON3 by human serum samples collected from malaria-endemic regions in Africa [ 23 , 24 ] was examined. ELISA plates (Nunc, Rochester, NY, USA) were coated with the recombinant protein (5 μg/ml, 50 μl per well) at 4°C overnight.…”

Section: Methodsmentioning

confidence: 99%

PfRON3 is an erythrocyte-binding protein and a potential blood-stage vaccine candidate antigen

Zhao

Chang

et al. 2014

Malar J

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BackgroundErythrocyte invasion by merozoites is an essential step in Plasmodium falciparum infection and leads to subsequent disease pathology. Proteins both on the merozoite surface and secreted from the apical organelles (micronemes, rhoptries and dense granules) mediate the invasion of erythrocytes; some of the molecules have been regarded as targets in the development of an anti-malaria vaccine. Recently, a subgroup of rhoptry neck proteins (PfRON2, PfRON4 and PfRON5) associated with the microneme protein apical membrane antigen AMA1 has been described as components of the moving junction complex that assists merozoite invasion into erythrocytes. However, unlike PfRON2, PfRON4 and PfRON5, the latest study suggested that PfRON3 might be located in the rhoptry bulb and participates in a novel PfRON complex (PfRON2, 3 and 4), but does not form a complex with AMA1. Additionally, the full-length PfRON3 protein possesses three transmembrane regions at the N-terminus, which is highly conserved among RON3 orthologues in the genus Plasmodium, Toxoplasma gondii and Eimeria tenella. Overall, these findings suggest that PfRON3 may play an important role in merozoite invasion into erythrocytes.ResultsPfRON3 was primarily expressed during the late trophozoite stage, with a peak in transcription levels at 40 hours post-invasion. The subcellular localization of PfRON3 was confirmed that it is a merozoite rhoptry bulb protein. Additionally, the recombinant form of PfRON3 protein bound to the erythrocyte and was recognized by sera collected from malaria endemic areas in Africa, and anti-PfRON3 antibodies significantly inhibited merozoite invasion into erythrocytes.MethodsThe expression of PfRON3 was analysed via real-time quantitative PCR, and the recombinant PfRON3 proteins were generated with an Escherichia coli expression system. The subcellular localization of PfRON3 was assessed with immunoelectron microscopy and immunofluorescence assay (IFA). The recognition PfRON3 by malaria immune sera was analysed with an enzyme-linked immunosorbent assay (ELISA). Erythrocyte-binding assays were performed using recombinant PfRON3 proteins and invasion inhibition assays were carried out with PfRON3-specific antibodies.ConclusionThis study confirmed that PfRON3 is a rhoptry protein with an erythrocyte-binding property, which is likely associated red blood cell invasion. PfRON3 is a potential vaccine candidate.Electronic supplementary materialThe online version of this article (doi:10.1186/1475-2875-13-490) contains supplementary material, which is available to authorized users.

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“…Other tested antigens are the following: two allelic variants of the merozoite surface antigen 2 (MSP2‐3D7 and MSP2‐FC27), which are involved in attachment of merozoite to erythrocytes [13]. The fourth antigen was the C‐terminal fragment (C231) of the Pf332 antigen [14], a target for opsonizing antibodies [5], and the latter were found to be efficient inhibitors of parasite growth in vitro [14–16]. The used plasma samples were collected in a middle of a dry season to avoid short‐term immune responses following acute malaria attacks.…”

Section: Introductionmentioning

confidence: 99%

“…The recombinant AMA‐1 and MSP2 antigens were kindly supplied by Dr. Robin Anders. The recombinant Pf332‐C231 corresponding to a 231 amino acids fragment in the C‐terminal part of Pf332 [14] was kindly supplied by Ms. Halima Balogun, Stockholm University. Bound IgG was detected with goat anti‐human IgG‐ALP (1:2000) (Mabtech, Nacka, Sweden).…”

mentioning

confidence: 99%

Pattern of Pre‐existing IgG Subclass Responses to a Panel of Asexual Stage Malaria Antigens Reported During the Lengthy Dry Season in Daraweesh, Sudan

et al. 2011

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The anti-malarial IgG immune response during the lengthy and dry season in areas of low malaria transmission as in Eastern Sudan is largely unknown. In this study, ELISA was used for the measurement of pre-existing total IgG and IgG subclasses to a panel of malaria antigens, MSP2-3D7, MSP2-FC27, AMA-1 and Pf332-C231. The results showed that the antibody responses were predominantly age dependent, antigen specific, and their lifespan was at least 5-6 month long. Generally, the IgG3 was most abundant IgG subclass, and the most recognized antigen was Pf332-C231. Furthermore, the correlation between the levels of IgG subclasses was strongest between IgG1 and IgG3, which were more predictive to the total IgG levels. Finally, the response pattern of each of the IgG subclasses to the different test antigens that were spanning the dry season and the correlation between these responses were described in details for the first time.

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Immunogenicity and antigenic properties of Pf332-C231, a fragment of a non-repeat region of the Plasmodium falciparum antigen Pf332

Cited by 8 publications

References 25 publications

Characterization of the Duffy-Binding-Like Domain ofPlasmodium falciparumBlood-Stage Antigen 332

Characterization of the Duffy-Binding-Like Domain ofPlasmodium falciparumBlood-Stage Antigen 332

PfRON3 is an erythrocyte-binding protein and a potential blood-stage vaccine candidate antigen

Pattern of Pre‐existing IgG Subclass Responses to a Panel of Asexual Stage Malaria Antigens Reported During the Lengthy Dry Season in Daraweesh, Sudan

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