Identification and polymorphism of Plasmodium vivax RBP-1 peptides which bind specifically to reticulocytes

Plasmodium vivax merozoite preferentially invades reticulocytes probably using PvRBP-1 as ligand. One hundred and ninety-five, 15-mer peptides has been synthesised from PvRBP-1 sequence; tested in reticulocyte- or erythrocyte-binding assays. Twenty-five peptides ( K d=76–380 nM) specifically defined...

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Veröffentlicht in:Peptides (New York, N.Y. : 1980) N.Y. : 1980), 2002-12, Vol.23 (12), p.2265-2277
Hauptverfasser: Urquiza, Mauricio, Patarroyo, Manuel A., Marı&#x0301, n, Viviana, Ocampo, Marisol, Suarez, Jorge, Lopez, Ramses, Puentes, Alvaro, Curtidor, Hernando, Garcı&#x0301, a, Javier, Rodrı&#x0301, guez, Luis E., Vera, Ricardo, Torres, Angela, Laverde, Marilu, Robles, Ana P., Patarroyo, Manuel E.
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Sprache:eng
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Zusammenfassung:Plasmodium vivax merozoite preferentially invades reticulocytes probably using PvRBP-1 as ligand. One hundred and ninety-five, 15-mer peptides has been synthesised from PvRBP-1 sequence; tested in reticulocyte- or erythrocyte-binding assays. Twenty-five peptides ( K d=76–380 nM) specifically defined four reticulocyte-binding regions. It has been reported that a highly conserved Region-I recombinant fragment binds specifically to reticulocytes. HABP-critical residues for reticulocyte-binding were highly conserved in 20 Colombian P. vivax clinical isolates, suggesting an important biological function. There were six overlapping reticulocyte-binding sites for these peptides according to enzyme sensitivity and mutual competition-binding assays; located on 26- and 41-kDa reticulocyte membrane surface proteins.
ISSN:0196-9781
1873-5169
DOI:10.1016/S0196-9781(02)00267-X