Characterisation of Plasmodium falciparum RESA-like protein peptides that bind specifically to erythrocytes and inhibit invasion

Luis Eduardo Rodriguez, Ricardo Vera, John Valbuena, Hernando Curtidor, Javier Garcia, Alvaro Puentes, Marisol Ocampo, Ramses Lopez, Jaiver Rosas, Yolanda Lopez, Manuel A. Patarroyo, Manuel E. Patarroyo

Resultado de la investigación: Contribución a RevistaArtículo

2 Citas (Scopus)

Resumen

The Plasmodium falciparum ring-erythrocyte surface antigen (RESA)-like putative protein was identified and characterised. PCR and RT-PCR assays revealed that the gene encoding this protein was both present and being transcribed in P. falciparum strain FCB-2 16 h after erythrocyte invasion. Indirect immunofluorescence studies detected this protein in infected erythrocyte (IE) cytosol in dense fluorescent granules similar to Maurer's clefts at 16-20 h (parasites in ring and trophozoite stages) and very strongly on IE membranes at 22 h, suggesting that it is synthesised during early ring stages (16 h) and transported to the infected red blood cell (RBC) membrane surface during the trophozoite stage (22 h). Western blotting showed that antisera produced against polymerised synthetic peptides of this protein recognised a 72-kDa band in P. falciparum schizont lysate. P. falciparum RESA-like peptides used in normal RBC binding assays revealed that peptides 30326 (101NAEKI LGFDD KNILE ALDLFY120), 30334 ( 281RVTWK KLRTK MIKAL KKSLTY300) and 30342 ( 431SSPQR LKFTA GGGFC GKLRNY450) bind with high activity and saturability, presenting nM affinity constants. These peptides contain α-helical structural elements, as determined by circular dichroism, and inhibit P. falciparum in vitro invasion of normal RBCs by up to 91%, suggesting that some RESA-like protein regions are involved in intra-erythrocyte stage P. falciparum invasion. ©2007 by Walter de Gruyter.
Idioma originalEnglish (US)
Páginas (desde-hasta)15-24
Número de páginas10
PublicaciónBiological Chemistry
Volumen388
N.º1
DOI
EstadoPublished - ene 1 2007
Publicado de forma externa

Huella dactilar

Plasmodium falciparum
Surface Antigens
Erythrocytes
Peptides
Proteins
Assays
Blood
Trophozoites
Gene encoding
Cell membranes
Immune Sera
Schizonts
Polymerase Chain Reaction
Erythrocyte Membrane
Membranes
Indirect Fluorescent Antibody Technique
Circular Dichroism
Cytosol
Parasites
Western Blotting

Citar esto

Rodriguez, L. E., Vera, R., Valbuena, J., Curtidor, H., Garcia, J., Puentes, A., ... Patarroyo, M. E. (2007). Characterisation of Plasmodium falciparum RESA-like protein peptides that bind specifically to erythrocytes and inhibit invasion. Biological Chemistry, 388(1), 15-24. https://doi.org/10.1515/BC.2007.002
Rodriguez, Luis Eduardo ; Vera, Ricardo ; Valbuena, John ; Curtidor, Hernando ; Garcia, Javier ; Puentes, Alvaro ; Ocampo, Marisol ; Lopez, Ramses ; Rosas, Jaiver ; Lopez, Yolanda ; Patarroyo, Manuel A. ; Patarroyo, Manuel E. / Characterisation of Plasmodium falciparum RESA-like protein peptides that bind specifically to erythrocytes and inhibit invasion. En: Biological Chemistry. 2007 ; Vol. 388, N.º 1. pp. 15-24.
@article{288a0feac2e44176ba40a2a68bec0d8e,
title = "Characterisation of Plasmodium falciparum RESA-like protein peptides that bind specifically to erythrocytes and inhibit invasion",
abstract = "The Plasmodium falciparum ring-erythrocyte surface antigen (RESA)-like putative protein was identified and characterised. PCR and RT-PCR assays revealed that the gene encoding this protein was both present and being transcribed in P. falciparum strain FCB-2 16 h after erythrocyte invasion. Indirect immunofluorescence studies detected this protein in infected erythrocyte (IE) cytosol in dense fluorescent granules similar to Maurer's clefts at 16-20 h (parasites in ring and trophozoite stages) and very strongly on IE membranes at 22 h, suggesting that it is synthesised during early ring stages (16 h) and transported to the infected red blood cell (RBC) membrane surface during the trophozoite stage (22 h). Western blotting showed that antisera produced against polymerised synthetic peptides of this protein recognised a 72-kDa band in P. falciparum schizont lysate. P. falciparum RESA-like peptides used in normal RBC binding assays revealed that peptides 30326 (101NAEKI LGFDD KNILE ALDLFY120), 30334 ( 281RVTWK KLRTK MIKAL KKSLTY300) and 30342 ( 431SSPQR LKFTA GGGFC GKLRNY450) bind with high activity and saturability, presenting nM affinity constants. These peptides contain α-helical structural elements, as determined by circular dichroism, and inhibit P. falciparum in vitro invasion of normal RBCs by up to 91{\%}, suggesting that some RESA-like protein regions are involved in intra-erythrocyte stage P. falciparum invasion. {\circledC}2007 by Walter de Gruyter.",
author = "Rodriguez, {Luis Eduardo} and Ricardo Vera and John Valbuena and Hernando Curtidor and Javier Garcia and Alvaro Puentes and Marisol Ocampo and Ramses Lopez and Jaiver Rosas and Yolanda Lopez and Patarroyo, {Manuel A.} and Patarroyo, {Manuel E.}",
year = "2007",
month = "1",
day = "1",
doi = "10.1515/BC.2007.002",
language = "English (US)",
volume = "388",
pages = "15--24",
journal = "Biological Chemistry",
issn = "1431-6730",
publisher = "Walter de Gruyter GmbH & Co. KG",
number = "1",

}

Rodriguez, LE, Vera, R, Valbuena, J, Curtidor, H, Garcia, J, Puentes, A, Ocampo, M, Lopez, R, Rosas, J, Lopez, Y, Patarroyo, MA & Patarroyo, ME 2007, 'Characterisation of Plasmodium falciparum RESA-like protein peptides that bind specifically to erythrocytes and inhibit invasion', Biological Chemistry, vol. 388, n.º 1, pp. 15-24. https://doi.org/10.1515/BC.2007.002

Characterisation of Plasmodium falciparum RESA-like protein peptides that bind specifically to erythrocytes and inhibit invasion. / Rodriguez, Luis Eduardo; Vera, Ricardo; Valbuena, John; Curtidor, Hernando; Garcia, Javier; Puentes, Alvaro; Ocampo, Marisol; Lopez, Ramses; Rosas, Jaiver; Lopez, Yolanda; Patarroyo, Manuel A.; Patarroyo, Manuel E.

En: Biological Chemistry, Vol. 388, N.º 1, 01.01.2007, p. 15-24.

Resultado de la investigación: Contribución a RevistaArtículo

TY - JOUR

T1 - Characterisation of Plasmodium falciparum RESA-like protein peptides that bind specifically to erythrocytes and inhibit invasion

AU - Rodriguez, Luis Eduardo

AU - Vera, Ricardo

AU - Valbuena, John

AU - Curtidor, Hernando

AU - Garcia, Javier

AU - Puentes, Alvaro

AU - Ocampo, Marisol

AU - Lopez, Ramses

AU - Rosas, Jaiver

AU - Lopez, Yolanda

AU - Patarroyo, Manuel A.

AU - Patarroyo, Manuel E.

PY - 2007/1/1

Y1 - 2007/1/1

N2 - The Plasmodium falciparum ring-erythrocyte surface antigen (RESA)-like putative protein was identified and characterised. PCR and RT-PCR assays revealed that the gene encoding this protein was both present and being transcribed in P. falciparum strain FCB-2 16 h after erythrocyte invasion. Indirect immunofluorescence studies detected this protein in infected erythrocyte (IE) cytosol in dense fluorescent granules similar to Maurer's clefts at 16-20 h (parasites in ring and trophozoite stages) and very strongly on IE membranes at 22 h, suggesting that it is synthesised during early ring stages (16 h) and transported to the infected red blood cell (RBC) membrane surface during the trophozoite stage (22 h). Western blotting showed that antisera produced against polymerised synthetic peptides of this protein recognised a 72-kDa band in P. falciparum schizont lysate. P. falciparum RESA-like peptides used in normal RBC binding assays revealed that peptides 30326 (101NAEKI LGFDD KNILE ALDLFY120), 30334 ( 281RVTWK KLRTK MIKAL KKSLTY300) and 30342 ( 431SSPQR LKFTA GGGFC GKLRNY450) bind with high activity and saturability, presenting nM affinity constants. These peptides contain α-helical structural elements, as determined by circular dichroism, and inhibit P. falciparum in vitro invasion of normal RBCs by up to 91%, suggesting that some RESA-like protein regions are involved in intra-erythrocyte stage P. falciparum invasion. ©2007 by Walter de Gruyter.

AB - The Plasmodium falciparum ring-erythrocyte surface antigen (RESA)-like putative protein was identified and characterised. PCR and RT-PCR assays revealed that the gene encoding this protein was both present and being transcribed in P. falciparum strain FCB-2 16 h after erythrocyte invasion. Indirect immunofluorescence studies detected this protein in infected erythrocyte (IE) cytosol in dense fluorescent granules similar to Maurer's clefts at 16-20 h (parasites in ring and trophozoite stages) and very strongly on IE membranes at 22 h, suggesting that it is synthesised during early ring stages (16 h) and transported to the infected red blood cell (RBC) membrane surface during the trophozoite stage (22 h). Western blotting showed that antisera produced against polymerised synthetic peptides of this protein recognised a 72-kDa band in P. falciparum schizont lysate. P. falciparum RESA-like peptides used in normal RBC binding assays revealed that peptides 30326 (101NAEKI LGFDD KNILE ALDLFY120), 30334 ( 281RVTWK KLRTK MIKAL KKSLTY300) and 30342 ( 431SSPQR LKFTA GGGFC GKLRNY450) bind with high activity and saturability, presenting nM affinity constants. These peptides contain α-helical structural elements, as determined by circular dichroism, and inhibit P. falciparum in vitro invasion of normal RBCs by up to 91%, suggesting that some RESA-like protein regions are involved in intra-erythrocyte stage P. falciparum invasion. ©2007 by Walter de Gruyter.

U2 - 10.1515/BC.2007.002

DO - 10.1515/BC.2007.002

M3 - Article

C2 - 17214545

VL - 388

SP - 15

EP - 24

JO - Biological Chemistry

JF - Biological Chemistry

SN - 1431-6730

IS - 1

ER -