Serine Repeat Antigen Peptides which bind specifically to Red Blood Cells.

Magnolia Vanegas Murcia; Alvaro Puentes; Jaime Alejandrino Garcia; Ricardo Vera-Bravo; Ramses Lopez; Mauricio Urquiza; Magnolia Vanegas Murcia; Luz Mary Salazar; Manuel Alfonso Patarroyo

Serine Repeat Antigen Peptides which bind specifically to Red Blood Cells.

Título traducido de la contribución: Péptidos de antígeno de repetición de serina que se unen específicamente a los glóbulos rojos.

Magnolia Vanegas Murcia, Alvaro Puentes, Jaime Alejandrino Garcia, Ricardo Vera-Bravo, Ramses Lopez, Mauricio Urquiza, Magnolia Vanegas Murcia, Luz Mary Salazar, Manuel Alfonso Patarroyo

Escuela de Medicina y Ciencias de la Salud

Producción científica: Contribución a una revista › Artículo › revisión exhaustiva

36 Citas (Scopus)

Resumen

Se ha informado que el antígeno de repetición de la serina (SERA) se une directamente a las membranas de los eritrocitos humanos, a las vesículas de dentro hacia fuera y a los eritrocitos de ratón intactos. De manera similar, los mAbs específicos contra SERA son efectivos para bloquear la invasión de glóbulos rojos (RBC) por merozoitos de P. falciparum. Además, el fragmento N-terminal recombinante SERA inhibe la invasión de eritrocitos por merozoitos. En este estudio de 49 péptidos de 20 residuos de longitud que no se superponen y que abarcan toda la cepa FCR3 de la proteína SERA, se encontraron siete péptidos con alta actividad de unión de los glóbulos rojos. Seis de estos péptidos (tres del dominio terminal SERA N) están localizados en regiones conservadas y muestran constantes de afinidad entre 150 y 1100 nM, coeficientes de colina entre 1.5 y 3.0 y 30000-120000 sitios de unión por célula. Algunos de estos péptidos inhibieron la invasión in vitro de eritrocitos y el desarrollo intra eritrocítico. Residuos que son críticos en la unión a los eritrocitos (en negrita), es decir 6725 (YLKETNNAISFESNSNSGSLEKK), 6733 (YALGSDIPEKCDTLASNCFLS), 6737 (YDNILVKMFKTNENNDKSELI), 6746 (DQGNCDTSWIFASKYHLETI), 6754 (YKKVQNLCGDDDTADHAVNIVG) y 6762 (NEVSERVHVYHILKHIKDGK), se determinaron mediante ensayos de competencia con péptidos análogos de glicina de alta fijación. La identificación de los péptidos que se unen a la membrana eritrocítica es importante para comprender el proceso de invasión de los glóbulos rojos por P.

Traducción realizada con el traductor www.DeepL.com/Translator

Título traducido de la contribución	Péptidos de antígeno de repetición de serina que se unen específicamente a los glóbulos rojos.
Idioma original	Inglés estadounidense
Número de artículo	49
Páginas (desde-hasta)	105 - 117
Publicación	Parasitology International
Estado	Publicada - 2000

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@article{b66afc587f9a4adc99c708672d6971fa,

title = "Serine Repeat Antigen Peptides which bind specifically to Red Blood Cells.",

abstract = "It has been reported that serine repeat antigen (SERA) binds directly to human erythrocyte membranes, inside-out vesicles and intact mouse erythrocytes. Similarly, mAbs specific against SERA are effective in blocking red blood cell (RBC) invasion by P. falciparum merozoites. Furthermore, the N-terminal recombinant SERA fragment inhibits the merozoite invasion of erythrocyte. In this study of 49 non-overlapping 20-residue-long peptides encompassing the whole SERA protein FCR3 strain, seven peptides having high RBC binding activity were found. Six of these peptides (three from the SERA N-terminal domain) are located in conserved regions and show affinity constants between 150 and 1100 nM, Hill coefficients between 1.5 and 3.0 and 30000-120000 binding sites per cell. Some of these peptides inhibited in vitro merozoite invasion of erythrocyte and intra-erythrocytic development. Residues which are critical in the binding to erythrocytes (in bold face), i.e. 6725 (YLKETNNAISFESNSGSLEKK), 6733 (YALGSDIPEKCDTLASNCFLS), 6737 (YDNILVKMFKTNENNDKSELI), 6746 (DQGNCDTSWIFASKYHLETI), 6754 (YKKVQNLCGDDTADHAVNIVG) and 6762 (NEVSERVHVYHILKHIKDGK), were determined by means of competition assays with high-binding peptide glycine analogues. The identification of peptides which bind to erythrocyte membrane is important in understanding the process of RBC invasion by P. ",

author = "{Vanegas Murcia}, Magnolia and Alvaro Puentes and Garcia, {Jaime Alejandrino} and Ricardo Vera-Bravo and Ramses Lopez and Mauricio Urquiza and {Vanegas Murcia}, Magnolia and Salazar, {Luz Mary} and Patarroyo, {Manuel Alfonso}",

year = "2000",

language = "English (US)",

pages = "105 -- 117",

journal = "Parasitology International",

issn = "1383-5769",

publisher = "Elsevier Ireland Ltd",

}

TY - JOUR

T1 - Serine Repeat Antigen Peptides which bind specifically to Red Blood Cells.

AU - Vanegas Murcia, Magnolia

AU - Puentes, Alvaro

AU - Garcia, Jaime Alejandrino

AU - Vera-Bravo, Ricardo

AU - Lopez, Ramses

AU - Urquiza, Mauricio

AU - Vanegas Murcia, Magnolia

AU - Salazar, Luz Mary

AU - Patarroyo, Manuel Alfonso

PY - 2000

Y1 - 2000

N2 - It has been reported that serine repeat antigen (SERA) binds directly to human erythrocyte membranes, inside-out vesicles and intact mouse erythrocytes. Similarly, mAbs specific against SERA are effective in blocking red blood cell (RBC) invasion by P. falciparum merozoites. Furthermore, the N-terminal recombinant SERA fragment inhibits the merozoite invasion of erythrocyte. In this study of 49 non-overlapping 20-residue-long peptides encompassing the whole SERA protein FCR3 strain, seven peptides having high RBC binding activity were found. Six of these peptides (three from the SERA N-terminal domain) are located in conserved regions and show affinity constants between 150 and 1100 nM, Hill coefficients between 1.5 and 3.0 and 30000-120000 binding sites per cell. Some of these peptides inhibited in vitro merozoite invasion of erythrocyte and intra-erythrocytic development. Residues which are critical in the binding to erythrocytes (in bold face), i.e. 6725 (YLKETNNAISFESNSGSLEKK), 6733 (YALGSDIPEKCDTLASNCFLS), 6737 (YDNILVKMFKTNENNDKSELI), 6746 (DQGNCDTSWIFASKYHLETI), 6754 (YKKVQNLCGDDTADHAVNIVG) and 6762 (NEVSERVHVYHILKHIKDGK), were determined by means of competition assays with high-binding peptide glycine analogues. The identification of peptides which bind to erythrocyte membrane is important in understanding the process of RBC invasion by P.

AB - It has been reported that serine repeat antigen (SERA) binds directly to human erythrocyte membranes, inside-out vesicles and intact mouse erythrocytes. Similarly, mAbs specific against SERA are effective in blocking red blood cell (RBC) invasion by P. falciparum merozoites. Furthermore, the N-terminal recombinant SERA fragment inhibits the merozoite invasion of erythrocyte. In this study of 49 non-overlapping 20-residue-long peptides encompassing the whole SERA protein FCR3 strain, seven peptides having high RBC binding activity were found. Six of these peptides (three from the SERA N-terminal domain) are located in conserved regions and show affinity constants between 150 and 1100 nM, Hill coefficients between 1.5 and 3.0 and 30000-120000 binding sites per cell. Some of these peptides inhibited in vitro merozoite invasion of erythrocyte and intra-erythrocytic development. Residues which are critical in the binding to erythrocytes (in bold face), i.e. 6725 (YLKETNNAISFESNSGSLEKK), 6733 (YALGSDIPEKCDTLASNCFLS), 6737 (YDNILVKMFKTNENNDKSELI), 6746 (DQGNCDTSWIFASKYHLETI), 6754 (YKKVQNLCGDDTADHAVNIVG) and 6762 (NEVSERVHVYHILKHIKDGK), were determined by means of competition assays with high-binding peptide glycine analogues. The identification of peptides which bind to erythrocyte membrane is important in understanding the process of RBC invasion by P.

M3 - Article

SN - 1383-5769

SP - 105

EP - 117

JO - Parasitology International

JF - Parasitology International

M1 - 49

ER -

Serine Repeat Antigen Peptides which bind specifically to Red Blood Cells.

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