Antibodies to repeated amino acid sequences in Pf155, a merozoite associated antigen of plasmodium falciparum

Berzins, Klavs; Perlmann, Hedvig; Wåhlin, B; Ruangjirachuporn, Wipaporn; Høgh, Birthe; Petersen, Eskild; Björkman, Anders; Perlmann, Peter

doi:10.1590/s0074-02761986000600013

Cited by 11 publications

(15 citation statements)

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“…As the major part of these antibodies recognize linear sequences in the C-terminal octapeptide repeat of the molecule, the results also imply that these repeats are responsible for an important part of the surface IF of infected erythrocytes. This corroborates previously published results (12,13).…”

Section: Discussionsupporting

confidence: 94%

“…The inhibitory titer of the total IgG fractions from these sera was low, but after addition of high amounts of the IgG fraction, a complete reinvasion inhibition was obtained (data not shown). From this observation and from the shape of the titration curves, it could be concluded that the IgG fractions contained no material that interfered with reinvasion inhibition as previously seen with some other inhibitory sera (8,13). Thus, the strong increase ('1000-fold) of the inhibitory titer of the IgG obtained by affinity purification on the infected RBCs reflects an enrichment of specific antibodies, the concentration of which was low in the total IgG fraction (0.1-0.3% of total IgG).…”

Section: Discussionsupporting

confidence: 74%

“…Affinity-purified human antibodies to this octapeptide were extremely efficient inhibitors of merozoite reinvasion in vitro. Taken together, these results suggest that the octapeptide is part of a major antigenic region of Pf155 (13) and, hence, is a possible target structure for the induction of protective immunity against P. falciparum merozoites.…”

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confidence: 67%

“…Thus, after lysis and centrifugation of the recombinant bacteria, almost all of the fusion protein was found in the supernatant. The latter was fractionated by gel filtration, and each fraction was assayed for fusion protein by using an ELISA with the octapeptide-specific mouse monoclonal antibody (13,19). Fractions 42-50 reacted strongly with the antibody (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Immunoblotting was performed by previously described methods (6,18) using an octapeptidespecific mouse monoclonal antibody fpr probing. The latter was produced by immunizing mice with the synthetic octapeptide Glu-Glu-Asn-Val-Glu-His-Asp-Ala coupled to the carrier protein keyhole limpet hemocyanine (13,19 (6,17).…”

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confidence: 99%

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Synthetic gene construct expressing a repeated and highly immunogenic epitope of the Plasmodium falciparum antigen Pf155.

Åslund¹,

Sjölander²,

Wahlgren³

et al. 1987

Proc. Natl. Acad. Sci. U.S.A.

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The Plasmodium falciparum-derived antigen Pfl55 contains two blocks of tandemly repeated amino acid sequences. A pair of complementary oligonucleotides, encoding the C-terminally located repeat Val-Glu-His-Asp-Ala-Glu-GluAsn, were synthesized. The oligonucleotides were polymerized by ligation, and the resulting multimers were cloned into an expression vector. One construct that contained four copies of the repeat was expressed in Escherichia coli. The product, a fusion protein, was soluble and produced in high amounts. It reacted in immunoblotting with a monoclonal antibody to a synthetic octapeptide (Glu-Glu-Asn-Val-Glu-His-Asp-Ala).

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Section: Discussionsupporting

confidence: 94%

Section: Discussionsupporting

confidence: 74%

mentioning

confidence: 67%

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

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