Plasmodium falciparum TryThrA antigen synthetic peptides block in vitro merozoite invasion to erythrocytes

Hernando Curtidor, Marisol Ocampo, Luis E. Rodríguez, Ramses López, Javier E. García, John Valbuena, Ricardo Vera, Álvaro Puentes, Jesus Leiton, Lina J. Cortes, Yolanda López, Manuel A. Patarroyo, Manuel E. Patarroyo

Resultado de la investigación: Contribución a una revistaArtículorevisión exhaustiva

16 Citas (Scopus)

Resumen

Tryptophan-threonine-rich antigen (TryThrA) is a Plasmodium falciparum homologue of Plasmodium yoelii-infected erythrocyte membrane pypAg-1 antigen. pypAg-1 binds to the surface of uninfected mouse erythrocytes and has been used successfully in vaccine studies. The two antigens are characterized by an unusual tryptophan-rich domain, suggesting similar biological properties. Using synthetic peptides spanning the TryThrA sequence and human erythrocyte we have done binding assays to identify possible TryThrA functional regions. We describe four peptides outside the tryptophan-rich domain having high activity binding to normal human erythrocytes. The peptides termed HABPs (high activity binding peptides) are 30884 (61LKEKKKKVLEFFENLVLNKKY80) located at the N-terminal and 30901 (401RKSLEQQFGDNMDKMNKLKKY420), 30902 (421KKILKFFPLFNYKSDLESIM440) and 30913 ( 641DLESTAEQKAEKKGGKAKAKY660) located at the C-terminal. Studies with polyclonal goat antiserum against synthetic peptides chosen to represent the whole length of the protein showed that TryThrA has fluorescence pattern similar to PypAg-1 of P. yoelii. All HABPs inhibited merozoite in vitro invasion, suggesting that TryThrA protein may be participating in merozoite-erythrocyte interaction during invasion. © 2005 Elsevier Inc. All rights reserved.
Idioma originalInglés estadounidense
Número de artículo3
Páginas (desde-hasta)888-896
Número de páginas9
PublicaciónBiochemical and Biophysical Research Communications
Volumen339
N.º3
DOI
EstadoPublicada - ene 20 2006
Publicado de forma externa

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