MAEBL Plasmodium falciparum protein peptides bind specifically to erythrocytes and inhibit in vitro merozoite invasion

Marisol Ocampo; Hernando Curtidor; Ricardo Vera; John J Valbuena; Luis E Rodríguez; Alvaro Puentes; Ramses López; Javier E García; Diana Tovar; Paola Pacheco; Miguel A Navarro; Manuel E Patarroyo

doi:10.1016/j.bbrc.2004.01.050

MAEBL Plasmodium falciparum protein peptides bind specifically to erythrocytes and inhibit in vitro merozoite invasion

Marisol Ocampo, Hernando Curtidor, Ricardo Vera, John J Valbuena, Luis E Rodríguez, Alvaro Puentes, Ramses López, Javier E García, Diana Tovar, Paola Pacheco, Miguel A Navarro, Manuel E Patarroyo

Escuela de Medicina y Ciencias de la Salud

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16 Citas (Scopus)

Resumen

MAEBL is an erythrocyte binding protein located in the rhoptries and on the surface of mature merozoites, being expressed at the beginning of schizogony. The structure of MAEBL originally isolated from rodent malaria parasites suggested a molecule likely to be involved in invasion. We thus became interested in identifying possible MAEBL functional regions. Synthetic peptides spanning the MAEBL sequence were tested in erythrocyte binding assays to identify such possible MAEBL functional regions. Nine high activity binding peptides (HABPs) were identified: two were found in the M1 domain, one was found between the M1 and M2 regions, five in the erythrocyte binding domain (M2), and one in the protein's repeat region. The results showed that peptide binding was saturable; some HABPs inhibited in vitro merozoite invasion and specifically bound to a 33kDa protein on red blood cell membrane. HABPs' possible function in merozoite invasion of erythrocytes is also discussed.

Idioma original	Inglés estadounidense
Páginas (desde-hasta)	319-29
Número de páginas	11
Publicación	Biochemical and Biophysical Research Communications
Volumen	315
N.º	2
DOI	https://doi.org/10.1016/j.bbrc.2004.01.050
Estado	Publicada - mar. 5 2004

ODS de las Naciones Unidas

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Ocampo, M., Curtidor, H., Vera, R., Valbuena, J. J., Rodríguez, L. E., Puentes, A., López, R., García, J. E., Tovar, D., Pacheco, P., Navarro, M. A., & Patarroyo, M. E. (2004). MAEBL Plasmodium falciparum protein peptides bind specifically to erythrocytes and inhibit in vitro merozoite invasion. Biochemical and Biophysical Research Communications, 315(2), 319-29. https://doi.org/10.1016/j.bbrc.2004.01.050

@article{be8ef6e225574e8e8c785c017e44c7eb,

title = "MAEBL Plasmodium falciparum protein peptides bind specifically to erythrocytes and inhibit in vitro merozoite invasion",

abstract = "MAEBL is an erythrocyte binding protein located in the rhoptries and on the surface of mature merozoites, being expressed at the beginning of schizogony. The structure of MAEBL originally isolated from rodent malaria parasites suggested a molecule likely to be involved in invasion. We thus became interested in identifying possible MAEBL functional regions. Synthetic peptides spanning the MAEBL sequence were tested in erythrocyte binding assays to identify such possible MAEBL functional regions. Nine high activity binding peptides (HABPs) were identified: two were found in the M1 domain, one was found between the M1 and M2 regions, five in the erythrocyte binding domain (M2), and one in the protein's repeat region. The results showed that peptide binding was saturable; some HABPs inhibited in vitro merozoite invasion and specifically bound to a 33kDa protein on red blood cell membrane. HABPs' possible function in merozoite invasion of erythrocytes is also discussed.",

author = "Marisol Ocampo and Hernando Curtidor and Ricardo Vera and Valbuena, {John J} and Rodr{\'i}guez, {Luis E} and Alvaro Puentes and Ramses L{\'o}pez and Garc{\'i}a, {Javier E} and Diana Tovar and Paola Pacheco and Navarro, {Miguel A} and Patarroyo, {Manuel E}",

year = "2004",

month = mar,

day = "5",

doi = "10.1016/j.bbrc.2004.01.050",

language = "English (US)",

volume = "315",

pages = "319--29",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Academic Press Inc.",

number = "2",

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Ocampo, M, Curtidor, H, Vera, R, Valbuena, JJ, Rodríguez, LE, Puentes, A, López, R, García, JE, Tovar, D, Pacheco, P, Navarro, MA & Patarroyo, ME 2004, 'MAEBL Plasmodium falciparum protein peptides bind specifically to erythrocytes and inhibit in vitro merozoite invasion', Biochemical and Biophysical Research Communications, vol. 315, n.º 2, pp. 319-29. https://doi.org/10.1016/j.bbrc.2004.01.050

TY - JOUR

T1 - MAEBL Plasmodium falciparum protein peptides bind specifically to erythrocytes and inhibit in vitro merozoite invasion

AU - Ocampo, Marisol

AU - Curtidor, Hernando

AU - Vera, Ricardo

AU - Valbuena, John J

AU - Rodríguez, Luis E

AU - Puentes, Alvaro

AU - López, Ramses

AU - García, Javier E

AU - Tovar, Diana

AU - Pacheco, Paola

AU - Navarro, Miguel A

AU - Patarroyo, Manuel E

PY - 2004/3/5

Y1 - 2004/3/5

N2 - MAEBL is an erythrocyte binding protein located in the rhoptries and on the surface of mature merozoites, being expressed at the beginning of schizogony. The structure of MAEBL originally isolated from rodent malaria parasites suggested a molecule likely to be involved in invasion. We thus became interested in identifying possible MAEBL functional regions. Synthetic peptides spanning the MAEBL sequence were tested in erythrocyte binding assays to identify such possible MAEBL functional regions. Nine high activity binding peptides (HABPs) were identified: two were found in the M1 domain, one was found between the M1 and M2 regions, five in the erythrocyte binding domain (M2), and one in the protein's repeat region. The results showed that peptide binding was saturable; some HABPs inhibited in vitro merozoite invasion and specifically bound to a 33kDa protein on red blood cell membrane. HABPs' possible function in merozoite invasion of erythrocytes is also discussed.

AB - MAEBL is an erythrocyte binding protein located in the rhoptries and on the surface of mature merozoites, being expressed at the beginning of schizogony. The structure of MAEBL originally isolated from rodent malaria parasites suggested a molecule likely to be involved in invasion. We thus became interested in identifying possible MAEBL functional regions. Synthetic peptides spanning the MAEBL sequence were tested in erythrocyte binding assays to identify such possible MAEBL functional regions. Nine high activity binding peptides (HABPs) were identified: two were found in the M1 domain, one was found between the M1 and M2 regions, five in the erythrocyte binding domain (M2), and one in the protein's repeat region. The results showed that peptide binding was saturable; some HABPs inhibited in vitro merozoite invasion and specifically bound to a 33kDa protein on red blood cell membrane. HABPs' possible function in merozoite invasion of erythrocytes is also discussed.

U2 - 10.1016/j.bbrc.2004.01.050

DO - 10.1016/j.bbrc.2004.01.050

M3 - Article

C2 - 14766210

SN - 0006-291X

VL - 315

SP - 319

EP - 329

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 2

ER -

MAEBL Plasmodium falciparum protein peptides bind specifically to erythrocytes and inhibit in vitro merozoite invasion

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