Comparative recognition by human IgG antibodies of recombinant proteins representing three asexual erythrocytic stage vaccine candidates of Plasmodium vivax

Barbedo, Mayara B; Ricci, Ricardo; Jimenez, Maria Carolina Sarti; Cunha, Mariana; Yazdani, Syed Shams; Chitnis, Chetan E.; Rodrigues, Maurício M.; Soares, Irene S.

doi:10.1590/s0074-02762007005000040

Cited by 38 publications

(48 citation statements)

References 17 publications

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“…Purified PvAMA-1 produced in E. coli and P. pastoris were examined by ELISA with sera collected from 208 individuals during patent P. vivax infection (25). The results showed that 72.7% and 62.5% of the sera recognized E. coli PvAMA-1 and P. pastoris PvAMA-1, respectively.…”

Section: Resultsmentioning

confidence: 99%

“…In previous studies, we showed that recombinant proteins expressed in E. coli based on the P. vivax AMA-1 sequence were recognized by IgG antibodies of a large fraction of malaria-infected individuals (23)(24)(25)(26). 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).…”

Section: Discussionmentioning

confidence: 96%

“…In previous studies, we have shown that recombinant proteins based on P. vivax AMA-1 are immunogenic in natural infection (23)(24)(25)(26). 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: 97%

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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: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 96%

mentioning

confidence: 97%

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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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“…Inhibitory antibodies specific for the 19-kD C-terminal of P. falciparum MSP-1 were not correlated with delayed appearance of infection but, actually, declined significantly in 2 months after treatment, which might have contributed to the risk of reinfection. 27,37 Herein, all individuals were infected at the time of sampling.…”

Section: Discussionmentioning

confidence: 99%

Evaluation of the Naturally Acquired Antibody Immune Response to the Pv200L N-terminal Fragment of Plasmodium vivax Merozoite Surface Protein-1 in Four Areas of the Amazon Region of Brazil

Storti-Melo¹,

Souza-Neiras²,

Cassiano³

et al. 2011

The American Journal of Tropical Medicine and Hygiene

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“…Anti-rPyM2-MAEBL antibodies titers were determined by enzyme-linked immunosorbent assay (ELISA) as previously described (32). Plates were coated with recombinant protein at 200 ng/well.…”

Section: Methodsmentioning

confidence: 99%

Immunization with the MAEBL M2 Domain Protects against Lethal Plasmodium yoelii Infection

et al. 2015

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Comparative recognition by human IgG antibodies of recombinant proteins representing three asexual erythrocytic stage vaccine candidates of Plasmodium vivax

Abstract: In previous immuno-epidemiological studies of the naturally acquired antibody responses to merozoite sur-

Cited by 38 publications

References 17 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

Evaluation of the Naturally Acquired Antibody Immune Response to the Pv200L N-terminal Fragment of Plasmodium vivax Merozoite Surface Protein-1 in Four Areas of the Amazon Region of Brazil

Immunization with the MAEBL M2 Domain Protects against Lethal Plasmodium yoelii Infection

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