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 RevistaArtículo

15 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 originalEnglish (US)
Número de artículo3
Páginas (desde-hasta)888-896
Número de páginas9
PublicaciónBiochemical and Biophysical Research Communications
Volumen339
N.º3
DOI
EstadoPublished - ene 20 2006
Publicado de forma externa

Huella dactilar

Merozoites
Synthetic Vaccines
Tryptophan
Erythrocytes
Threonine
Antigens
Peptides
Plasmodium yoelii
Erythrocyte Membrane
Plasmodium falciparum
In Vitro Techniques
Plasmodium falciparum TryThrA antigen
Goats
Immune Sera
Assays
Proteins
Vaccines
Fluorescence
Membranes

Citar esto

Curtidor, H., Ocampo, M., Rodríguez, L. E., López, R., García, J. E., Valbuena, J., ... Patarroyo, M. E. (2006). Plasmodium falciparum TryThrA antigen synthetic peptides block in vitro merozoite invasion to erythrocytes. Biochemical and Biophysical Research Communications, 339(3), 888-896. [3]. https://doi.org/10.1016/j.bbrc.2005.11.089
Curtidor, Hernando ; Ocampo, Marisol ; Rodríguez, Luis E. ; López, Ramses ; García, Javier E. ; Valbuena, John ; Vera, Ricardo ; Puentes, Álvaro ; Leiton, Jesus ; Cortes, Lina J. ; López, Yolanda ; Patarroyo, Manuel A. ; Patarroyo, Manuel E. / Plasmodium falciparum TryThrA antigen synthetic peptides block in vitro merozoite invasion to erythrocytes. En: Biochemical and Biophysical Research Communications. 2006 ; Vol. 339, N.º 3. pp. 888-896.
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title = "Plasmodium falciparum TryThrA antigen synthetic peptides block in vitro merozoite invasion to erythrocytes",
abstract = "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. {\circledC} 2005 Elsevier Inc. All rights reserved.",
author = "Hernando Curtidor and Marisol Ocampo and Rodr{\'i}guez, {Luis E.} and Ramses L{\'o}pez and Garc{\'i}a, {Javier E.} and John Valbuena and Ricardo Vera and {\'A}lvaro Puentes and Jesus Leiton and Cortes, {Lina J.} and Yolanda L{\'o}pez and Patarroyo, {Manuel A.} and Patarroyo, {Manuel E.}",
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Curtidor, H, Ocampo, M, Rodríguez, LE, López, R, García, JE, Valbuena, J, Vera, R, Puentes, Á, Leiton, J, Cortes, LJ, López, Y, Patarroyo, MA & Patarroyo, ME 2006, 'Plasmodium falciparum TryThrA antigen synthetic peptides block in vitro merozoite invasion to erythrocytes', Biochemical and Biophysical Research Communications, vol. 339, n.º 3, 3, pp. 888-896. https://doi.org/10.1016/j.bbrc.2005.11.089

Plasmodium falciparum TryThrA antigen synthetic peptides block in vitro merozoite invasion to erythrocytes. / Curtidor, Hernando; Ocampo, Marisol; Rodríguez, Luis E.; López, Ramses; García, Javier E.; Valbuena, John; Vera, Ricardo; Puentes, Álvaro; Leiton, Jesus; Cortes, Lina J.; López, Yolanda; Patarroyo, Manuel A.; Patarroyo, Manuel E.

En: Biochemical and Biophysical Research Communications, Vol. 339, N.º 3, 3, 20.01.2006, p. 888-896.

Resultado de la investigación: Contribución a RevistaArtículo

TY - JOUR

T1 - Plasmodium falciparum TryThrA antigen synthetic peptides block in vitro merozoite invasion to erythrocytes

AU - Curtidor, Hernando

AU - Ocampo, Marisol

AU - Rodríguez, Luis E.

AU - López, Ramses

AU - García, Javier E.

AU - Valbuena, John

AU - Vera, Ricardo

AU - Puentes, Álvaro

AU - Leiton, Jesus

AU - Cortes, Lina J.

AU - López, Yolanda

AU - Patarroyo, Manuel A.

AU - Patarroyo, Manuel E.

PY - 2006/1/20

Y1 - 2006/1/20

N2 - 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.

AB - 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.

U2 - 10.1016/j.bbrc.2005.11.089

DO - 10.1016/j.bbrc.2005.11.089

M3 - Article

C2 - 16329993

VL - 339

SP - 888

EP - 896

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 3

M1 - 3

ER -