Specific erythrocyte binding capacity and biological activity of Plasmodium falciparum erythrocyte binding ligand 1 (EBL-1)-derived peptides

Hernando Curtidor; Luis E Rodríguez; Marisol Ocampo; Ramses López; Javier E García; John Valbuena; Ricardo Vera; Alvaro Puentes; Magnolia Vanegas; Manuel E Patarroyo

doi:10.1110/ps.041084305

Specific erythrocyte binding capacity and biological activity of Plasmodium falciparum erythrocyte binding ligand 1 (EBL-1)-derived peptides

Hernando Curtidor, Luis E Rodríguez, Marisol Ocampo, Ramses López, Javier E García, John Valbuena, Ricardo Vera, Alvaro Puentes, Magnolia Vanegas, Manuel E Patarroyo

Research output: Contribution to journal › Research Article › peer-review

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Abstract

Erythrocyte binding ligand 1 (EBL-1) is a member of the ebl multigene family involved in Plasmodium falciparum invasion of erythrocytes. We found that five EBL-1 high-activity binding peptides (HABPs) bound specifically to erythrocytes: 29895 ((41)HKKKSGELNNNKSGILRSTY(60)), 29903 ((201)LYECGK-KIKEMKWICTDNQF(220)), 29923 ((601)CNAILGSYADIGDIVRGLDV(620)), 29924((621)WRDINTNKLSEK-FQKIFMGGY(640)), and 30018 ((2481)LEDIINLSKKKKKSINDTSFY(2500)). We also show that binding was saturable, not sialic acid-dependent, and that all peptides specifically bound to a 36-kDa protein on the erythrocyte membrane. The five HABPs inhibited in vitro merozoite invasion depending on the peptide concentration used, suggesting their possible role in the invasion process.

Original language	English (US)
Pages (from-to)	464 - 473
Number of pages	10
Journal	Protein Science
Volume	14
Issue number	2
DOIs	https://doi.org/10.1110/ps.041084305
State	Published - Feb 2005

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title = "Specific erythrocyte binding capacity and biological activity of Plasmodium falciparum erythrocyte binding ligand 1 (EBL-1)-derived peptides",

abstract = "Erythrocyte binding ligand 1 (EBL-1) is a member of the ebl multigene family involved in Plasmodium falciparum invasion of erythrocytes. We found that five EBL-1 high-activity binding peptides (HABPs) bound specifically to erythrocytes: 29895 ((41)HKKKSGELNNNKSGILRSTY(60)), 29903 ((201)LYECGK-KIKEMKWICTDNQF(220)), 29923 ((601)CNAILGSYADIGDIVRGLDV(620)), 29924((621)WRDINTNKLSEK-FQKIFMGGY(640)), and 30018 ((2481)LEDIINLSKKKKKSINDTSFY(2500)). We also show that binding was saturable, not sialic acid-dependent, and that all peptides specifically bound to a 36-kDa protein on the erythrocyte membrane. The five HABPs inhibited in vitro merozoite invasion depending on the peptide concentration used, suggesting their possible role in the invasion process.",

author = "Hernando Curtidor and Rodr{\'i}guez, {Luis E} and Marisol Ocampo and Ramses L{\'o}pez and Garc{\'i}a, {Javier E} and John Valbuena and Ricardo Vera and Alvaro Puentes and Magnolia Vanegas and Patarroyo, {Manuel E}",

year = "2005",

month = feb,

doi = "10.1110/ps.041084305",

language = "English (US)",

volume = "14",

pages = "464 -- 473",

journal = "Protein Science",

issn = "0961-8368",

publisher = "Cold Spring Harbor Laboratory Press",

number = "2",

}

TY - JOUR

T1 - Specific erythrocyte binding capacity and biological activity of Plasmodium falciparum erythrocyte binding ligand 1 (EBL-1)-derived peptides

AU - Curtidor, Hernando

AU - Rodríguez, Luis E

AU - Ocampo, Marisol

AU - López, Ramses

AU - García, Javier E

AU - Valbuena, John

AU - Vera, Ricardo

AU - Puentes, Alvaro

AU - Vanegas, Magnolia

AU - Patarroyo, Manuel E

PY - 2005/2

Y1 - 2005/2

N2 - Erythrocyte binding ligand 1 (EBL-1) is a member of the ebl multigene family involved in Plasmodium falciparum invasion of erythrocytes. We found that five EBL-1 high-activity binding peptides (HABPs) bound specifically to erythrocytes: 29895 ((41)HKKKSGELNNNKSGILRSTY(60)), 29903 ((201)LYECGK-KIKEMKWICTDNQF(220)), 29923 ((601)CNAILGSYADIGDIVRGLDV(620)), 29924((621)WRDINTNKLSEK-FQKIFMGGY(640)), and 30018 ((2481)LEDIINLSKKKKKSINDTSFY(2500)). We also show that binding was saturable, not sialic acid-dependent, and that all peptides specifically bound to a 36-kDa protein on the erythrocyte membrane. The five HABPs inhibited in vitro merozoite invasion depending on the peptide concentration used, suggesting their possible role in the invasion process.

AB - Erythrocyte binding ligand 1 (EBL-1) is a member of the ebl multigene family involved in Plasmodium falciparum invasion of erythrocytes. We found that five EBL-1 high-activity binding peptides (HABPs) bound specifically to erythrocytes: 29895 ((41)HKKKSGELNNNKSGILRSTY(60)), 29903 ((201)LYECGK-KIKEMKWICTDNQF(220)), 29923 ((601)CNAILGSYADIGDIVRGLDV(620)), 29924((621)WRDINTNKLSEK-FQKIFMGGY(640)), and 30018 ((2481)LEDIINLSKKKKKSINDTSFY(2500)). We also show that binding was saturable, not sialic acid-dependent, and that all peptides specifically bound to a 36-kDa protein on the erythrocyte membrane. The five HABPs inhibited in vitro merozoite invasion depending on the peptide concentration used, suggesting their possible role in the invasion process.

U2 - 10.1110/ps.041084305

DO - 10.1110/ps.041084305

M3 - Research Article

C2 - 15659376

SN - 0961-8368

VL - 14

SP - 464

EP - 473

JO - Protein Science

JF - Protein Science

IS - 2

ER -

Specific erythrocyte binding capacity and biological activity of Plasmodium falciparum erythrocyte binding ligand 1 (EBL-1)-derived peptides

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