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 una revistaArtículorevisión exhaustiva

3 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 originalInglés estadounidense
Páginas (desde-hasta)15-24
Número de páginas10
PublicaciónBiological Chemistry
Volumen388
N.º1
DOI
EstadoPublicada - ene 1 2007
Publicado de forma externa

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