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
        }
}
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21 Citations
Background Citations
4
Methods Citations
2

21 Citations

Citation Type

Citation Type

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.
Purification of the integral membrane glycoproteins D of herpes simplex virus types 1 and 2, produced in the recombinant baculovirus expression system, by ion-exchange high-performance liquid chromatography.
Detergent extraction of herpes simplex virus type 1 glycoprotein D by zwitterionic and non-ionic detergents and purification by ion-exchange high-performance liquid chromatography.
Differential localization of full-length and processed forms of PF83/AMA-1 an apical membrane antigen of Plasmodium falciparum merozoites.
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.
Induction of anti-malarial transmission blocking immunity with a recombinant ookinete surface antigen of Plasmodium berghei produced in silkworm larvae using the baculovirus expression vector system.
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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References

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Analysis of variation in PF83, an erythrocytic merozoite vaccine candidate antigen of Plasmodium falciparum.
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TLDR
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TLDR
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