Non-allele specific antibody responses to genetically distinct variant forms of Plasmodium vivax Duffy binding protein (PvDBP-II) in Iranians exposed to seasonal malaria transmission

Valizadeh, Vahideh; Zakeri, Sedigheh; Mehrizi, Akram Abouie; Djadid, Navid Dinparast

doi:10.1016/j.actatropica.2014.03.019

Cited by 10 publications

(30 citation statements)

References 61 publications

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“…Based on a previous study [34], five genetically distinct variants of PvDBP-II were selected (DBPI, DBPV, DBPVI, DBPIX, and DBPX with GenBank accession nos. EU860428.1, EU860432.1, EU860433.1, EU860436.1, and KF318358, respectively).…”

Section: Selection Of the Five Different Variant Forms Of The Pvdbp-iimentioning

confidence: 99%

“…For human sera, 20 patients' sera infected with P. vivax (15 males and 5 females, age range between 10 and 62 years, mean age: 28.5) were selected from 202 collected P. vivax-infected human's sera on the basis of infected parasite sequence type and also from OD ≥ 1 of anti-PvDBP-II-IgG based on ELISA results [34]. In this test, various dilutions of sera (1:10, 1:20, 1:50, and 1:100) were examined to determine the best dilution for performing EBIA.…”

Section: Erythrocyte-binding Inhibition Assaymentioning

confidence: 99%

“…Moreover, naturally cross-reactive antibodies to the five expressed allelic forms of PvDBP-II were detected among individuals who are living in malaria-endemic areas of Iran by using immune-depletion assay [34]. Therefore, the present investigation was designed to determine whether naturally cross-reactive antibodies have immune protective activity that could have functional inhibitory effects on binding of all five PvDBP-II variant forms expressed on the surface of COS-7 cells to Duffy-positive RBC.…”

Section: Introductionmentioning

confidence: 98%

“…Interestingly, it has been reported that the essential domains or regions for binding to RBC are less polymorphic. These conserved regions may be suitable targets for cross-reactive antibodies [34][35][36], and antibodies to these conserved regions could inhibit binding of different variant forms of DBP-II to RBC and overcome the problem of antigenic diversity for designing a broadly effective vaccine.…”

Section: Introductionmentioning

confidence: 99%

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Natural acquired inhibitory antibodies to Plasmodium vivax Duffy binding protein (PvDBP-II) equally block erythrocyte binding of homologous and heterologous expressed PvDBP-II on the surface of COS-7 cells

Valizadeh

Zakeri

Mehrizi

et al. 2015

Med Microbiol Immunol

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The binding domain of Plasmodium vivax Duffy binding protein (PvDBP-II) is a promising blood-stage vaccine candidate for vivax malaria. For the development of a successful vivax malaria vaccine based on DBP-II, the antigenic diversity and also naturally occurring functional antibodies to different PvDBP-II variant types in the various populations must be determined. However, similar to other blood-stage antigens, allelic variation within the PvDBP-II is a fundamental challenge for the development of a broadly efficient vaccine. The present study was performed to define whether the polymorphisms in PvDBP-II influence the nature of functional inhibitory activity of naturally acquired or induced anti-DBP-II antibodies in mice. In this investigation, five genetically distinct variants of PvDBP-II were transiently expressed on the COS-7 cell surface. Erythrocyte-binding inhibition assay (EBIA) was performed using human sera infected with corresponding and non-corresponding P. vivax variants as well as by the use of mice sera immunized with different expressed recombinant PvDBP-IIs. EBIA results showed that the inhibitory percentage varied between 50 and 63 % by using sera from infected individuals, and in case of mouse antisera, inhibition was in the range of 76-86 %. Interestingly, no significant difference was detected in red blood cell binding inhibition when different PvDBP-II variants on the COS-7 cell surfaces were incubated with heterologous and homologous sera infected with PvDBP-II variants. This suggests that the detected polymorphisms in all five forms of PvDBP-II may not affect functional activity of anti-DBP-II antibodies. In conclusion, our results revealed that there are functional cross-reactive antibody responses to heterologous PvDBP-II variants that might provide a broader inhibitory response against all, or at least the majority of strains compared to single allele of this protein that should be considered in development of PvDBP-II-based vaccine.

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Section: Selection Of the Five Different Variant Forms Of The Pvdbp-iimentioning

confidence: 99%

Section: Erythrocyte-binding Inhibition Assaymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Natural acquired inhibitory antibodies to Plasmodium vivax Duffy binding protein (PvDBP-II) equally block erythrocyte binding of homologous and heterologous expressed PvDBP-II on the surface of COS-7 cells

Valizadeh

Zakeri

Mehrizi

et al. 2015

Med Microbiol Immunol

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“…DBP-IX is identical to reference strain, Sal-1 (accession number, M61095) which has implication for vaccine research studies. DBP-IX was cloned in pQE30 vector (Qiagen, Hilden, Germany) and expressed in E. coli M15 strain as recombinant protein fused to the histidine tag as described previously [15]. Briefly, overnight culture of E. coli M15pQE30-DBP-IX was grown in Luria broth (pH~7.2) containing ampicillin (100 μg/ml) and kanamycine (25 μg/mL) at 37°C with shaking (150 rpm) until an optical density (OD) of 0.6-0.7 at 600 nm was reached.…”

Section: Study Area and Subjectsmentioning

confidence: 99%

Optimized Method for Purification of Expressed Plasmodium Vivax Duffy Binding Protein-II (PvDBP-II): Implication for Vivax Malaria Vaccine Development

Valizadeh

Mirkazemi

Vaziri

et al. 2014

vacres

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Insights into the naturally acquired immune response toPlasmodium vivaxmalaria

2016

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Plasmodium vivax is the most geographically widespread of the malaria parasites causing human disease, yet it is comparatively understudied compared with Plasmodium falciparum. In this article we review what is known about naturally acquired immunity to P. vivax, and importantly, how this differs to that acquired against P. falciparum. Immunity to clinical P. vivax infection is acquired more quickly than to P. falciparum, and evidence suggests humans in endemic areas also have a greater capacity to mount a successful immunological memory response to this pathogen. Both of these factors give promise to the idea of a successful P. vivax vaccine. We review what is known about both the cellular and humoral immune response, including the role of cytokines, antibodies, immunoregulation, immune memory and immune dysfunction. Furthermore, we discuss where the future lies in terms of advancing our understanding of naturally acquired immunity to P. vivax, through the use of well-designed longitudinal epidemiological studies and modern tools available to immunologists.

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Non-allele specific antibody responses to genetically distinct variant forms of Plasmodium vivax Duffy binding protein (PvDBP-II) in Iranians exposed to seasonal malaria transmission

Cited by 10 publications

References 61 publications

Natural acquired inhibitory antibodies to Plasmodium vivax Duffy binding protein (PvDBP-II) equally block erythrocyte binding of homologous and heterologous expressed PvDBP-II on the surface of COS-7 cells

Natural acquired inhibitory antibodies to Plasmodium vivax Duffy binding protein (PvDBP-II) equally block erythrocyte binding of homologous and heterologous expressed PvDBP-II on the surface of COS-7 cells

Optimized Method for Purification of Expressed Plasmodium Vivax Duffy Binding Protein-II (PvDBP-II): Implication for Vivax Malaria Vaccine Development

Insights into the naturally acquired immune response toPlasmodium vivaxmalaria

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