Ion-exchange-immunoaffinity purification of a recombinant baculovirus Plasmodium falciparum apical membrane antigen, PF83/AMA-1.

@article{Narum1993IonexchangeimmunoaffinityPO,
  title={Ion-exchange-immunoaffinity purification of a recombinant baculovirus Plasmodium falciparum apical membrane antigen, PF83/AMA-1.},
  author={David L. Narum and Gjalt W. Welling and A. W. Thomas},
  journal={Journal of chromatography. A},
  year={1993},
  volume={657 2},
  pages={
          357-63
        }
}
High prevalence of natural antibodies against Plasmodium falciparum 83-kilodalton apical membrane antigen (PF83/AMA-1) as detected by capture-enzyme-linked immunosorbent assay using full-length baculovirus recombinant PF83/AMA-1.
TLDR
Analysis of populations from villages in Guinea-Bissau and in an area of high malarial transmission in Senegal demonstrated a very high prevalence of naturally acquired serum IgG responses to PF83/AMA-1, showing that PF83-7G8-1 may be a well-recognized asexual parasite antigen.
Purification, Characterization, and Immunogenicity of the Refolded Ectodomain of the Plasmodium falciparum Apical Membrane Antigen 1 Expressed in Escherichia coli
TLDR
The process described here was successfully scaled up to produce AMA1/E protein under GMP conditions, and the product was found to induce highly inhibitory antibodies in rabbits.
Baculovirus-mediated expression of Plasmodium falciparum erythrocyte binding antigen 175 polypeptides and their recognition by human antibodies
TLDR
The results suggest that these regions of the EBA-175 protein are targets for the immune response against malaria and support their further study as possible vaccine components.
Proteolytic Processing and Primary Structure ofPlasmodium falciparum Apical Membrane Antigen-1*
TLDR
Direct microsequencing and mass spectrometric peptide mass fingerprinting are used to characterize in detail the primary structure and proteolytic processing of PfAMA-1 and have shown that both species possess a completely intact and unmodified transmembrane and cytoplasmic domain.
Precise Timing of Expression of a Plasmodium falciparum-derived Transgene in Plasmodium berghei Is a Critical Determinant of Subsequent Subcellular Localization*
TLDR
Heterologous (trans-species) expression of the human malaria Plasmodium falciparum AMA-1 (PF83/AMA-1) in the rodent parasite P. berghei was highly immunogenic in mice, resulting in a response against a functionally critical domain of the molecule.
Aspects of immunity for the AMA-1 family of molecules in humans and non-human primates malarias.
TLDR
The use of an eukaryotic full length recombinant PF83/AMA-1 molecule is described to develop a sensitive ELISA for the determination of serological responses in endemic populations, which reveals surprisingly high levels of humoral response to this quantitatively minor antigen.
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Inhibition was not associated with detectable damage to intracellular parasites, suggesting that the inhibitory monoclonal antibodies act by blocking the reinfection of red cells by newly released merozoites, suggesting potential interest as a vaccine against P. knowlesi malaria.
Sixty‐six kilodalton‐related antigens of Plasmodium knowlesi are merozoite surface antigens associated with the apical prominence
TLDR
The observations suggest that 66 kD‐related antigens may play a role in the orientation of the apical prominence of merozoites towards the red cell, and/or in the junction formation that occurs subsequent to orientation.
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