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; Álvaro 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, Álvaro Puentes, Magnolia Vanegas, Manuel E. Patarroyo

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12 Citas (Scopus)

Resumen

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 (⁴¹HKKKSGELNNNKSGILRSTY⁶⁰), 29903 (²⁰¹LYECGKKIKEMKWICTDNQF²²⁰), 29923 ( ⁶⁰¹CNAILGSYADIGDIVRGLDV⁶²⁰), 29924( ⁶²¹WRDINTNKLSEKFQKIFMGGY⁶⁴⁰), and 30018 ( ²⁴⁸¹LEDIINLSKKKKKSINDTSFY²⁵⁰⁰). 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.

Idioma original	Inglés
Páginas (desde-hasta)	464-473
Número de páginas	10
Publicación	Protein Science
Volumen	14
N.º	2
DOI	https://doi.org/10.1110/ps.041084305
Estado	Publicada - feb. 2005
Publicado de forma externa	Sí

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@article{003e22267329477d8cb3a921e299cf0d,

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 (41HKKKSGELNNNKSGILRSTY60), 29903 (201LYECGKKIKEMKWICTDNQF220), 29923 ( 601CNAILGSYADIGDIVRGLDV620), 29924( 621WRDINTNKLSEKFQKIFMGGY640), and 30018 ( 2481LEDIINLSKKKKKSINDTSFY2500). 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.",

keywords = "Erythrocyte binding ligand-1, Malaria protein, Peptides, Plasmodium falciparum",

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 {\'A}lvaro Puentes and Magnolia Vanegas and Patarroyo, {Manuel E.}",

year = "2005",

month = feb,

doi = "10.1110/ps.041084305",

language = "English",

volume = "14",

pages = "464--473",

journal = "Protein Science",

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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, Álvaro

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 (41HKKKSGELNNNKSGILRSTY60), 29903 (201LYECGKKIKEMKWICTDNQF220), 29923 ( 601CNAILGSYADIGDIVRGLDV620), 29924( 621WRDINTNKLSEKFQKIFMGGY640), and 30018 ( 2481LEDIINLSKKKKKSINDTSFY2500). 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 (41HKKKSGELNNNKSGILRSTY60), 29903 (201LYECGKKIKEMKWICTDNQF220), 29923 ( 601CNAILGSYADIGDIVRGLDV620), 29924( 621WRDINTNKLSEKFQKIFMGGY640), and 30018 ( 2481LEDIINLSKKKKKSINDTSFY2500). 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.

KW - Erythrocyte binding ligand-1

KW - Malaria protein

KW - Peptides

KW - Plasmodium falciparum

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U2 - 10.1110/ps.041084305

DO - 10.1110/ps.041084305

M3 - Article

C2 - 15659376

AN - SCOPUS:19944431632

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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