Plasmodium vivax: functional analysis of a highlyconserved PvRBP-1 protein region.

Manuel Alfonso Patarroyo; Elvia María Cantor; Tania Bibiana Lombo; Libia Alexandra Cepeda; Manuel Elkin Patarroyo; Ana María Espinosa; Carlos Alberto Barrero; Fanny Guzmán; María L. Gunturiz; Mauricio Urquiza; Marisol Ocampo Cifuentes

Plasmodium vivax: functional analysis of a highlyconserved PvRBP-1 protein region.

Manuel Alfonso Patarroyo
, Elvia María Cantor
, Tania Bibiana Lombo
, Libia Alexandra Cepeda
, Manuel Elkin Patarroyo
, Ana María Espinosa
, Carlos Alberto Barrero
, Fanny Guzmán
, María L. Gunturiz
, Mauricio Urquiza
, Marisol Ocampo Cifuentes

Escuela de Medicina y Ciencias de la Salud

Producción científica: Contribución a revista › Artículo de Investigación › revisión exhaustiva

Resumen

Plasmodium iax is one of the most prevalent malarial species around the world [1]. Two P. iax reticulocyte binding proteins (PvRBP-1 and PvRBP-2),
expressed at the apical pole of this parasite, are considered to be the binding ligands involved in the specific
selection of this younger red blood cell population [2].
The adhesion of the PvRBP complex, to an unknown
receptor on the target cells, does not depend on the
presence of the red blood cell Duffy glycoprotein, this
being strictly a receptor for the PvDBP protein

Idioma original	Inglés estadounidense
Páginas (desde-hasta)	229 - 234
Número de páginas	6
Publicación	Molecular and Biochemical Parasitology
Volumen	1
N.º	117
Estado	Publicada - 2001

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Patarroyo, M. A., Cantor, E. M., Lombo, T. B., Cepeda, L. A., Patarroyo, M. E., Espinosa, A. M., Barrero, C. A., Guzmán, F., Gunturiz, M. L., Urquiza, M., & Ocampo Cifuentes, M. (2001). Plasmodium vivax: functional analysis of a highlyconserved PvRBP-1 protein region. Molecular and Biochemical Parasitology, 1(117), 229 - 234. https://www.sciencedirect.com/sdfe/pdf/download/eid/1-s2.0-S0166685101003553/first-page-pdf

@article{5763ed1f819f40a8816d89e28749b12a,

title = "Plasmodium vivax: functional analysis of a highlyconserved PvRBP-1 protein region.",

abstract = "Plasmodium iax is one of the most prevalent malarial species around the world [1]. Two P. iax reticulocyte binding proteins (PvRBP-1 and PvRBP-2), expressed at the apical pole of this parasite, are considered to be the binding ligands involved in the specific selection of this younger red blood cell population [2]. The adhesion of the PvRBP complex, to an unknown receptor on the target cells, does not depend on the presence of the red blood cell Duffy glycoprotein, this being strictly a receptor for the PvDBP protein",

author = "Patarroyo, \{Manuel Alfonso\} and Cantor, \{Elvia Mar{\'i}a\} and Lombo, \{Tania Bibiana\} and Cepeda, \{Libia Alexandra\} and Patarroyo, \{Manuel Elkin\} and Espinosa, \{Ana Mar{\'i}a\} and Barrero, \{Carlos Alberto\} and Fanny Guzm{\'a}n and Gunturiz, \{Mar{\'i}a L.\} and Mauricio Urquiza and \{Ocampo Cifuentes\}, Marisol",

year = "2001",

language = "English (US)",

volume = "1",

pages = "229 -- 234",

journal = "Molecular and Biochemical Parasitology",

issn = "0166-6851",

publisher = "Elsevier BV",

number = "117",

}

Patarroyo, MA, Cantor, EM, Lombo, TB, Cepeda, LA, Patarroyo, ME, Espinosa, AM, Barrero, CA, Guzmán, F, Gunturiz, ML, Urquiza, M & Ocampo Cifuentes, M 2001, 'Plasmodium vivax: functional analysis of a highlyconserved PvRBP-1 protein region.', Molecular and Biochemical Parasitology, vol. 1, n.º 117, pp. 229 - 234. <https://www.sciencedirect.com/sdfe/pdf/download/eid/1-s2.0-S0166685101003553/first-page-pdf>

TY - JOUR

T1 - Plasmodium vivax: functional analysis of a highlyconserved PvRBP-1 protein region.

AU - Patarroyo, Manuel Alfonso

AU - Cantor, Elvia María

AU - Lombo, Tania Bibiana

AU - Cepeda, Libia Alexandra

AU - Patarroyo, Manuel Elkin

AU - Espinosa, Ana María

AU - Barrero, Carlos Alberto

AU - Guzmán, Fanny

AU - Gunturiz, María L.

AU - Urquiza, Mauricio

AU - Ocampo Cifuentes, Marisol

PY - 2001

Y1 - 2001

N2 - Plasmodium iax is one of the most prevalent malarial species around the world [1]. Two P. iax reticulocyte binding proteins (PvRBP-1 and PvRBP-2), expressed at the apical pole of this parasite, are considered to be the binding ligands involved in the specific selection of this younger red blood cell population [2]. The adhesion of the PvRBP complex, to an unknown receptor on the target cells, does not depend on the presence of the red blood cell Duffy glycoprotein, this being strictly a receptor for the PvDBP protein

AB - Plasmodium iax is one of the most prevalent malarial species around the world [1]. Two P. iax reticulocyte binding proteins (PvRBP-1 and PvRBP-2), expressed at the apical pole of this parasite, are considered to be the binding ligands involved in the specific selection of this younger red blood cell population [2]. The adhesion of the PvRBP complex, to an unknown receptor on the target cells, does not depend on the presence of the red blood cell Duffy glycoprotein, this being strictly a receptor for the PvDBP protein

M3 - Research Article

SN - 0166-6851

VL - 1

SP - 229

EP - 234

JO - Molecular and Biochemical Parasitology

JF - Molecular and Biochemical Parasitology

IS - 117

ER -

Plasmodium vivax: functional analysis of a highlyconserved PvRBP-1 protein region.

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