Identifying Plasmodium falciparum EBA-175 homologue sequences that specifically bind to human erythrocytes

John Jairo Valbuena; Ricardo Vera Bravo; Marisol Ocampo; Ramses Lopez; Luis E Rodriguez; Hernando Curtidor; Alvaro Puentes; Javier E Garcia; Diana Tovar; Johana Gomez; Jesus Leiton; Manuel Elkin Patarroyo

doi:10.1016/j.bbrc.2004.07.034

Identifying Plasmodium falciparum EBA-175 homologue sequences that specifically bind to human erythrocytes

John Jairo Valbuena, Ricardo Vera Bravo, Marisol Ocampo, Ramses Lopez, Luis E Rodriguez, Hernando Curtidor, Alvaro Puentes, Javier E Garcia, Diana Tovar, Johana Gomez, Jesus Leiton, Manuel Elkin Patarroyo

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6 Citas (Scopus)

Resumen

Erythrocyte binding antigen-160 (EBA-160) protein is a Plasmodium falciparum antigen homologue from the erythrocyte binding protein family (EBP). It has been shown that the EBP family plays a role in parasite binding to the erythrocyte surface. The EBA-160 sequence has been chemically synthesised in seventy 20-mer sequential peptides covering the entire 3D7 protein strain, each of which was tested in erythrocyte binding assays to identify possible EBA-160 functional regions. Five EBA-160 high activity binding peptides (HABPs) specifically binding to erythrocytes with high affinity were identified. Dissociation constants lay between 200 and 460 nM and Hill coefficients between 1.5 and 2.3. Erythrocyte membrane protein binding peptide cross-linking assays using SDS-PAGE showed that these peptides bound specifically to 12, 28, and 44 kDa erythrocyte membrane proteins. The nature of these receptor sites was studied in peptide binding assays using enzyme-treated erythrocytes. HABPs were able to block merozoite in vitro invasion of erythrocytes. HABPs' potential as anti-malarial vaccine candidates is also discussed.

Idioma original	Inglés estadounidense
Páginas (desde-hasta)	835-44
Número de páginas	10
Publicación	Biochemical and Biophysical Research Communications
Volumen	321
N.º	4
DOI	https://doi.org/10.1016/j.bbrc.2004.07.034
Estado	Publicada - sep. 3 2004

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Valbuena, J. J., Bravo, R. V., Ocampo, M., Lopez, R., Rodriguez, L. E., Curtidor, H., Puentes, A., Garcia, J. E., Tovar, D., Gomez, J., Leiton, J., & Patarroyo, M. E. (2004). Identifying Plasmodium falciparum EBA-175 homologue sequences that specifically bind to human erythrocytes. Biochemical and Biophysical Research Communications, 321(4), 835-44. https://doi.org/10.1016/j.bbrc.2004.07.034

@article{39c505445c31474a8ee2f99ac128148e,

title = "Identifying Plasmodium falciparum EBA-175 homologue sequences that specifically bind to human erythrocytes",

abstract = "Erythrocyte binding antigen-160 (EBA-160) protein is a Plasmodium falciparum antigen homologue from the erythrocyte binding protein family (EBP). It has been shown that the EBP family plays a role in parasite binding to the erythrocyte surface. The EBA-160 sequence has been chemically synthesised in seventy 20-mer sequential peptides covering the entire 3D7 protein strain, each of which was tested in erythrocyte binding assays to identify possible EBA-160 functional regions. Five EBA-160 high activity binding peptides (HABPs) specifically binding to erythrocytes with high affinity were identified. Dissociation constants lay between 200 and 460 nM and Hill coefficients between 1.5 and 2.3. Erythrocyte membrane protein binding peptide cross-linking assays using SDS-PAGE showed that these peptides bound specifically to 12, 28, and 44 kDa erythrocyte membrane proteins. The nature of these receptor sites was studied in peptide binding assays using enzyme-treated erythrocytes. HABPs were able to block merozoite in vitro invasion of erythrocytes. HABPs' potential as anti-malarial vaccine candidates is also discussed.",

author = "Valbuena, {John Jairo} and Bravo, {Ricardo Vera} and Marisol Ocampo and Ramses Lopez and Rodriguez, {Luis E} and Hernando Curtidor and Alvaro Puentes and Garcia, {Javier E} and Diana Tovar and Johana Gomez and Jesus Leiton and Patarroyo, {Manuel Elkin}",

year = "2004",

month = sep,

day = "3",

doi = "10.1016/j.bbrc.2004.07.034",

language = "English (US)",

volume = "321",

pages = "835--44",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Academic Press Inc.",

number = "4",

}

Valbuena, JJ, Bravo, RV, Ocampo, M, Lopez, R, Rodriguez, LE, Curtidor, H, Puentes, A, Garcia, JE, Tovar, D, Gomez, J, Leiton, J & Patarroyo, ME 2004, 'Identifying Plasmodium falciparum EBA-175 homologue sequences that specifically bind to human erythrocytes', Biochemical and Biophysical Research Communications, vol. 321, n.º 4, pp. 835-44. https://doi.org/10.1016/j.bbrc.2004.07.034

TY - JOUR

T1 - Identifying Plasmodium falciparum EBA-175 homologue sequences that specifically bind to human erythrocytes

AU - Valbuena, John Jairo

AU - Bravo, Ricardo Vera

AU - Ocampo, Marisol

AU - Lopez, Ramses

AU - Rodriguez, Luis E

AU - Curtidor, Hernando

AU - Puentes, Alvaro

AU - Garcia, Javier E

AU - Tovar, Diana

AU - Gomez, Johana

AU - Leiton, Jesus

AU - Patarroyo, Manuel Elkin

PY - 2004/9/3

Y1 - 2004/9/3

N2 - Erythrocyte binding antigen-160 (EBA-160) protein is a Plasmodium falciparum antigen homologue from the erythrocyte binding protein family (EBP). It has been shown that the EBP family plays a role in parasite binding to the erythrocyte surface. The EBA-160 sequence has been chemically synthesised in seventy 20-mer sequential peptides covering the entire 3D7 protein strain, each of which was tested in erythrocyte binding assays to identify possible EBA-160 functional regions. Five EBA-160 high activity binding peptides (HABPs) specifically binding to erythrocytes with high affinity were identified. Dissociation constants lay between 200 and 460 nM and Hill coefficients between 1.5 and 2.3. Erythrocyte membrane protein binding peptide cross-linking assays using SDS-PAGE showed that these peptides bound specifically to 12, 28, and 44 kDa erythrocyte membrane proteins. The nature of these receptor sites was studied in peptide binding assays using enzyme-treated erythrocytes. HABPs were able to block merozoite in vitro invasion of erythrocytes. HABPs' potential as anti-malarial vaccine candidates is also discussed.

AB - Erythrocyte binding antigen-160 (EBA-160) protein is a Plasmodium falciparum antigen homologue from the erythrocyte binding protein family (EBP). It has been shown that the EBP family plays a role in parasite binding to the erythrocyte surface. The EBA-160 sequence has been chemically synthesised in seventy 20-mer sequential peptides covering the entire 3D7 protein strain, each of which was tested in erythrocyte binding assays to identify possible EBA-160 functional regions. Five EBA-160 high activity binding peptides (HABPs) specifically binding to erythrocytes with high affinity were identified. Dissociation constants lay between 200 and 460 nM and Hill coefficients between 1.5 and 2.3. Erythrocyte membrane protein binding peptide cross-linking assays using SDS-PAGE showed that these peptides bound specifically to 12, 28, and 44 kDa erythrocyte membrane proteins. The nature of these receptor sites was studied in peptide binding assays using enzyme-treated erythrocytes. HABPs were able to block merozoite in vitro invasion of erythrocytes. HABPs' potential as anti-malarial vaccine candidates is also discussed.

U2 - 10.1016/j.bbrc.2004.07.034

DO - 10.1016/j.bbrc.2004.07.034

M3 - Article

C2 - 15358103

SN - 0006-291X

VL - 321

SP - 835

EP - 844

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 4

ER -

Identifying Plasmodium falciparum EBA-175 homologue sequences that specifically bind to human erythrocytes

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