P. falciparum pro-histoaspartic protease (proHAP) protein peptides bind specifically to erythrocytes and inhibit the invasion process in vitro

John Valbuena, Ricardo Vera, Alvaro Puentes, Marisol Ocampo, Javier Garcia, Hernando Curtidor, Ramses Lopez, Luis Rodriguez, Jaiver Rosas, Jimena Cortes, Martha Forero, Martha Pinto, Manuel Elkin Patarroyo

Resultado de la investigación: Contribución a RevistaArtículo

1 Cita (Scopus)

Resumen

Plasmodium falciparum histoaspartic protease (HAP) is an active enzyme involved in haemoglobin degradation. HAP is expressed as an inactive 51-kDa zymogen and is cleaved into an active 37-kDa enzyme. It has been proposed that this kind of protease might be implicated in the parasite's invasion of erythrocytes; however, this protein's role during invasion has still to be determined. Synthetic peptides derived from the HAP precursor (proHAP) were tested in erythrocyte binding assays to identify their possible function in the invasion process. Two proHAP high-activity binding peptides (HABPs) specifically bound to erythrocytes; these peptides were numbered 30609 (101LKNYIKESVKLFNKGLTKKS120) and 30610 (121YLGSEFDNVELKDLANVLSF140 ). The binding of these two peptides was saturable, presenting nanomolar affinity constants. These peptides interacted with 26- and 45-kDa proteins on the erythrocyte surface; the nature of these receptor sites was studied in peptide binding assays using enzyme-treated erythrocytes. The HABPs showed greater than 90% merozoite invasion inhibition in in vitro assays. Goat serum containing proHAP polymeric peptide antibodies inhibited parasite invasion in vitro .

Idioma originalEnglish (US)
Páginas (desde-hasta)361-7
Número de páginas7
PublicaciónBiological Chemistry
Volumen386
N.º4
DOI
EstadoPublished - jul 5 2005
Publicado de forma externa

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Valbuena, John ; Vera, Ricardo ; Puentes, Alvaro ; Ocampo, Marisol ; Garcia, Javier ; Curtidor, Hernando ; Lopez, Ramses ; Rodriguez, Luis ; Rosas, Jaiver ; Cortes, Jimena ; Forero, Martha ; Pinto, Martha ; Patarroyo, Manuel Elkin. / P. falciparum pro-histoaspartic protease (proHAP) protein peptides bind specifically to erythrocytes and inhibit the invasion process in vitro. En: Biological Chemistry. 2005 ; Vol. 386, N.º 4. pp. 361-7.
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abstract = "Plasmodium falciparum histoaspartic protease (HAP) is an active enzyme involved in haemoglobin degradation. HAP is expressed as an inactive 51-kDa zymogen and is cleaved into an active 37-kDa enzyme. It has been proposed that this kind of protease might be implicated in the parasite's invasion of erythrocytes; however, this protein's role during invasion has still to be determined. Synthetic peptides derived from the HAP precursor (proHAP) were tested in erythrocyte binding assays to identify their possible function in the invasion process. Two proHAP high-activity binding peptides (HABPs) specifically bound to erythrocytes; these peptides were numbered 30609 (101LKNYIKESVKLFNKGLTKKS120) and 30610 (121YLGSEFDNVELKDLANVLSF140 ). The binding of these two peptides was saturable, presenting nanomolar affinity constants. These peptides interacted with 26- and 45-kDa proteins on the erythrocyte surface; the nature of these receptor sites was studied in peptide binding assays using enzyme-treated erythrocytes. The HABPs showed greater than 90{\%} merozoite invasion inhibition in in vitro assays. Goat serum containing proHAP polymeric peptide antibodies inhibited parasite invasion in vitro .",
author = "John Valbuena and Ricardo Vera and Alvaro Puentes and Marisol Ocampo and Javier Garcia and Hernando Curtidor and Ramses Lopez and Luis Rodriguez and Jaiver Rosas and Jimena Cortes and Martha Forero and Martha Pinto and Patarroyo, {Manuel Elkin}",
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Valbuena, J, Vera, R, Puentes, A, Ocampo, M, Garcia, J, Curtidor, H, Lopez, R, Rodriguez, L, Rosas, J, Cortes, J, Forero, M, Pinto, M & Patarroyo, ME 2005, 'P. falciparum pro-histoaspartic protease (proHAP) protein peptides bind specifically to erythrocytes and inhibit the invasion process in vitro', Biological Chemistry, vol. 386, n.º 4, pp. 361-7. https://doi.org/10.1515/BC.2005.043

P. falciparum pro-histoaspartic protease (proHAP) protein peptides bind specifically to erythrocytes and inhibit the invasion process in vitro. / Valbuena, John; Vera, Ricardo; Puentes, Alvaro; Ocampo, Marisol; Garcia, Javier; Curtidor, Hernando; Lopez, Ramses; Rodriguez, Luis; Rosas, Jaiver; Cortes, Jimena; Forero, Martha; Pinto, Martha; Patarroyo, Manuel Elkin.

En: Biological Chemistry, Vol. 386, N.º 4, 05.07.2005, p. 361-7.

Resultado de la investigación: Contribución a RevistaArtículo

TY - JOUR

T1 - P. falciparum pro-histoaspartic protease (proHAP) protein peptides bind specifically to erythrocytes and inhibit the invasion process in vitro

AU - Valbuena, John

AU - Vera, Ricardo

AU - Puentes, Alvaro

AU - Ocampo, Marisol

AU - Garcia, Javier

AU - Curtidor, Hernando

AU - Lopez, Ramses

AU - Rodriguez, Luis

AU - Rosas, Jaiver

AU - Cortes, Jimena

AU - Forero, Martha

AU - Pinto, Martha

AU - Patarroyo, Manuel Elkin

PY - 2005/7/5

Y1 - 2005/7/5

N2 - Plasmodium falciparum histoaspartic protease (HAP) is an active enzyme involved in haemoglobin degradation. HAP is expressed as an inactive 51-kDa zymogen and is cleaved into an active 37-kDa enzyme. It has been proposed that this kind of protease might be implicated in the parasite's invasion of erythrocytes; however, this protein's role during invasion has still to be determined. Synthetic peptides derived from the HAP precursor (proHAP) were tested in erythrocyte binding assays to identify their possible function in the invasion process. Two proHAP high-activity binding peptides (HABPs) specifically bound to erythrocytes; these peptides were numbered 30609 (101LKNYIKESVKLFNKGLTKKS120) and 30610 (121YLGSEFDNVELKDLANVLSF140 ). The binding of these two peptides was saturable, presenting nanomolar affinity constants. These peptides interacted with 26- and 45-kDa proteins on the erythrocyte surface; the nature of these receptor sites was studied in peptide binding assays using enzyme-treated erythrocytes. The HABPs showed greater than 90% merozoite invasion inhibition in in vitro assays. Goat serum containing proHAP polymeric peptide antibodies inhibited parasite invasion in vitro .

AB - Plasmodium falciparum histoaspartic protease (HAP) is an active enzyme involved in haemoglobin degradation. HAP is expressed as an inactive 51-kDa zymogen and is cleaved into an active 37-kDa enzyme. It has been proposed that this kind of protease might be implicated in the parasite's invasion of erythrocytes; however, this protein's role during invasion has still to be determined. Synthetic peptides derived from the HAP precursor (proHAP) were tested in erythrocyte binding assays to identify their possible function in the invasion process. Two proHAP high-activity binding peptides (HABPs) specifically bound to erythrocytes; these peptides were numbered 30609 (101LKNYIKESVKLFNKGLTKKS120) and 30610 (121YLGSEFDNVELKDLANVLSF140 ). The binding of these two peptides was saturable, presenting nanomolar affinity constants. These peptides interacted with 26- and 45-kDa proteins on the erythrocyte surface; the nature of these receptor sites was studied in peptide binding assays using enzyme-treated erythrocytes. The HABPs showed greater than 90% merozoite invasion inhibition in in vitro assays. Goat serum containing proHAP polymeric peptide antibodies inhibited parasite invasion in vitro .

U2 - 10.1515/BC.2005.043

DO - 10.1515/BC.2005.043

M3 - Article

VL - 386

SP - 361

EP - 367

JO - Biological Chemistry

JF - Biological Chemistry

SN - 1431-6730

IS - 4

ER -