Long-Term Humoral and Cellular Immune Responses Elicited by a Heterologous Plasmodium vivax Apical Membrane Antigen 1 Protein Prime/Adenovirus Boost Immunization Protocol

Bouillet, Leoneide Érica Maduro; Dias, Magno; Dorigo, Natalia A.; Moura, Andrew D.; Russell, Bruce; Nosten, François; Rénia, Laurent; Braga, Érika Martins; Gazzinelli, Ricardo T.; Rodrigues, Maurício M.; Soares, Irene S.; Bruna-Romero, Oscar

doi:10.1128/iai.05048-11

Cited by 30 publications

(26 citation statements)

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“…We also described that these recombinant proteins can induce high antibody titers in mice following a homologous (protein-protein) or heterologous (protein-adenovirus) regimen of vaccination (27). Unfortunately, when produced in E. coli, the ectodomain of PvAMA-1 is insoluble and requires denaturation and refolding for purification (23,26).…”

Section: Discussionmentioning

confidence: 99%

“…Immunofluorescence assays were performed as described previously (27). Merozoite preparations were made from ex vivo matured and concentrated schizonts as described in the section v below.…”

Section: Methodsmentioning

confidence: 99%

“…Furthermore, a prime-boost strategy using recombinant AMA-1 administered in Montanide ISA720, followed by booster injection of AdHu5 expressing PvAMA-1, produced high titers of long-lasting antibodies and specific memory T cells (27).…”

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confidence: 99%

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Invasion-Inhibitory Antibodies Elicited by Immunization with Plasmodium vivax Apical Membrane Antigen-1 Expressed in Pichia pastoris Yeast

et al. 2014

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h In a recent vaccine trial performed with African children, immunization with a recombinant protein based on Plasmodium falciparum apical membrane antigen 1 (AMA-1) conferred a significant degree of strain-specific resistance against malaria. To contribute to the efforts of generating a vaccine against Plasmodium vivax malaria, we expressed the ectodomain of P. vivax AMA-1 (PvAMA-1) as a secreted soluble protein in the methylotrophic yeast Pichia pastoris. Recognized by a high percentage of sera from individuals infected by P. vivax, this recombinant protein was found to have maintained its antigenicity. The immunogenicity of this protein was evaluated in mice using immunization protocols that included homologous and heterologous primeboost strategies with plasmid DNA and recombinant protein. We used the following formulations containing different adjuvants: aluminum salts (Alum), Bordetella pertussis monophosphoryl lipid A (MPLA), flagellin FliC from Salmonella enterica serovar Typhimurium, saponin Quil A, or incomplete Freund's adjuvant (IFA). The formulations containing the adjuvants Quil A or IFA elicited the highest IgG antibody titers. Significant antibody titers were also obtained using a formulation developed for human use containing MPLA or Alum plus MPLA. Recombinant PvAMA-1 produced under "conditions of good laboratory practice" provided a good yield, high purity, low endotoxin levels, and no microbial contaminants and reproduced the experimental immunizations. Most relevant for vaccine development was the fact that immunization with PvAMA-1 elicited invasioninhibitory antibodies against different Asian isolates of P. vivax. Our results show that AMA-1 expressed in P. pastoris is a promising antigen for use in future preclinical and clinical studies.

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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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Invasion-Inhibitory Antibodies Elicited by Immunization with Plasmodium vivax Apical Membrane Antigen-1 Expressed in Pichia pastoris Yeast

et al. 2014

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“…Recently, Bouillet et al [68] have studied immunogenicty of PvAMA1 using adenovirus and recombinant protein in different prime boost regimens. The 'Protein/Ad' group (protein formulated with Montanide ISA720 followed by Ad5PvAMA1) elicited long-lasting PvAMA1-specific antibody responses, as well as memory T cell responses [68]. PvAMA-1 has also been expressed as a secreted protein in Pichia pastoris [69].…”

Section: P Vivax Apical Merozoite Antigen 1 (Pvama1)mentioning

confidence: 99%

Development of vaccines for Plasmodium vivax malaria

Müeller

Shakri

Chitnis

2015

Vaccine

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Plasmodium vivax continues to cause significant morbidity outside Africa with more than 50% of malaria cases in many parts of South and South-east Asia, Pacific islands, Central and South America being attributed to P. vivax infections. The unique biology of P. vivax, including its ability to form latent hypnozoites that emerge months to years later to cause blood stage infections, early appearance of gametocytes before clinical symptoms are apparent and a shorter development cycle in the vector makes elimination of P. vivax using standard control tools difficult. The availability of an effective vaccine that provides protection and prevents transmission would be a valuable tool in efforts to eliminate P. vivax. Here, we review the latest developments related to P. vivax malaria vaccines and discuss the challenges as well as directions toward the goal of developing highly efficacious vaccines against P. vivax malaria.

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“…A number of pre-clinical studies in mice and non-human primates were performed using these recombinant antigens. These pre-clinical studies used recombinant or synthetic antigens based on the CSP, MSP-1, AMA-1, and Duffy-binding protein [21]–[27].…”

Section: Introductionmentioning

confidence: 99%

Antigenicity and Immunogenicity of Plasmodium vivax Merozoite Surface Protein-3

et al. 2013

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A recent clinical trial in African children demonstrated the potential utility of merozoite surface protein (MSP)-3 as a vaccine against Plasmodium falciparum malaria. The present study evaluated the use of Plasmodium vivax MSP-3 (PvMSP-3) as a target antigen in vaccine formulations against malaria caused by P. vivax. Recombinant proteins representing MSP-3α and MSP-3β of P. vivax were expressed as soluble histidine-tagged bacterial fusions. Antigenicity during natural infection was evaluated by detecting specific antibodies using sera from individuals living in endemic areas of Brazil. A large proportion of infected individuals presented IgG antibodies to PvMSP-3α (68.2%) and at least 1 recombinant protein representing PvMSP-3β (79.1%). In spite of the large responder frequency, reactivity to both antigens was significantly lower than was observed for the immunodominant epitope present on the 19-kDa C-terminal region of PvMSP-1. Immunogenicity of the recombinant proteins was studied in mice in the absence or presence of different adjuvant formulations. PvMSP-3β, but not PvMSP-3α, induced a TLR4-independent humoral immune response in the absence of any adjuvant formulation. The immunogenicity of the recombinant antigens were also tested in formulations containing different adjuvants (Alum, Salmonella enterica flagellin, CpG, Quil A,TiterMax® and incomplete Freunds adjuvant) and combinations of two adjuvants (Alum plus flagellin, and CpG plus flagellin). Recombinant PvMSP-3α and PvMSP-3β elicited higher antibody titers capable of recognizing P. vivax-infected erythrocytes harvested from malaria patients. Our results confirm that P. vivax MSP-3 antigens are immunogenic during natural infection, and the corresponding recombinant proteins may be useful in elucidating their vaccine potential.

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Long-Term Humoral and Cellular Immune Responses Elicited by a Heterologous Plasmodium vivax Apical Membrane Antigen 1 Protein Prime/Adenovirus Boost Immunization Protocol

Cited by 30 publications

References 57 publications

Invasion-Inhibitory Antibodies Elicited by Immunization with Plasmodium vivax Apical Membrane Antigen-1 Expressed in Pichia pastoris Yeast

Invasion-Inhibitory Antibodies Elicited by Immunization with Plasmodium vivax Apical Membrane Antigen-1 Expressed in Pichia pastoris Yeast

Development of vaccines for Plasmodium vivax malaria

Antigenicity and Immunogenicity of Plasmodium vivax Merozoite Surface Protein-3

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