Plasmodium falciparum TryThrA antigen synthetic peptides block in vitro merozoite invasion to erythrocytes
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...
- Autores:
- Tipo de recurso:
- Fecha de publicación:
- 2006
- Institución:
- Universidad del Rosario
- Repositorio:
- Repositorio EdocUR - U. Rosario
- Idioma:
- eng
- OAI Identifier:
- oai:repository.urosario.edu.co:10336/25978
- Acceso en línea:
- https://doi.org/10.1016/j.bbrc.2005.11.089
https://repository.urosario.edu.co/handle/10336/25978
- Palabra clave:
- Peptides
Tryptophan-threonine-rich antigen
Plasmodium falciparum
Malaria
Invasion
- Rights
- License
- Restringido (Acceso a grupos específicos)
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oai:repository.urosario.edu.co:10336/25978 |
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EDOCUR2 |
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Repositorio EdocUR - U. Rosario |
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91225589-1ef6547b6-3130-435a-8a09-7ca050cd7b64-15e82e691-ba88-4d28-b934-b924d1350834-1d955461b-ddf3-4124-87c6-4ae101d2757d-14255e3fa-2b0d-47ce-ab18-c66a1b12d04d-134b82e95-53e0-4ba5-a5c5-d4191164afa1-1f2d05f42-2948-4c51-8389-8c3817c2d0f1-1b1a9fc9e-f3c2-4a42-9f4e-59db363b0583-1f0030114-3de7-419e-93c0-b849f5bf98f5-15566b76c-9e92-4ce1-94bb-1d122c35ea36-179653065-110ecd4f9-843f-4ef2-bec0-7d39d3381a13-1518488266002020-08-06T16:20:22Z2020-08-06T16:20:22Z2006-01-20Tryptophan–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.application/pdfhttps://doi.org/10.1016/j.bbrc.2005.11.089ISSN: 0006-291XEISSN: 1090-2104https://repository.urosario.edu.co/handle/10336/25978engElsevier896No. 3888Biochemical and Biophysical Research CommunicationsVol. 339Biochemical and Biophysical Research Communications, ISSN: 0006-291X;EISSN: 1090-2104, Vol.339, No.3 (2006); pp.888-896https://www.sciencedirect.com/science/article/abs/pii/S0006291X05026240Restringido (Acceso a grupos específicos)http://purl.org/coar/access_right/c_16ecBiochemical and Biophysical Research Communicationsinstname:Universidad del Rosarioreponame:Repositorio Institucional EdocURPeptidesTryptophan-threonine-rich antigenPlasmodium falciparumMalariaInvasionPlasmodium falciparum TryThrA antigen synthetic peptides block in vitro merozoite invasion to erythrocytesLos péptidos sintéticos antígeno TryThrA de Plasmodium falciparum bloquean la invasión in vitro de merozoitos a los eritrocitosarticleArtículohttp://purl.org/coar/version/c_970fb48d4fbd8a85http://purl.org/coar/resource_type/c_6501Curtidor, HernandoRodríguez, Luis E.López, RamsesGarc??a, Javier E.Valbuena, JohnVera, RicardoPuentes, ÁlvaroLeiton, JesusCortes, Lina J.López, YolandaPatarroyo, Manuel A.Patarroyo, Manuel E.Ocampo, Marisol10336/25978oai:repository.urosario.edu.co:10336/259782021-06-03 00:50:22.77https://repository.urosario.edu.coRepositorio institucional EdocURedocur@urosario.edu.co |
dc.title.spa.fl_str_mv |
Plasmodium falciparum TryThrA antigen synthetic peptides block in vitro merozoite invasion to erythrocytes |
dc.title.TranslatedTitle.spa.fl_str_mv |
Los péptidos sintéticos antígeno TryThrA de Plasmodium falciparum bloquean la invasión in vitro de merozoitos a los eritrocitos |
title |
Plasmodium falciparum TryThrA antigen synthetic peptides block in vitro merozoite invasion to erythrocytes |
spellingShingle |
Plasmodium falciparum TryThrA antigen synthetic peptides block in vitro merozoite invasion to erythrocytes Peptides Tryptophan-threonine-rich antigen Plasmodium falciparum Malaria Invasion |
title_short |
Plasmodium falciparum TryThrA antigen synthetic peptides block in vitro merozoite invasion to erythrocytes |
title_full |
Plasmodium falciparum TryThrA antigen synthetic peptides block in vitro merozoite invasion to erythrocytes |
title_fullStr |
Plasmodium falciparum TryThrA antigen synthetic peptides block in vitro merozoite invasion to erythrocytes |
title_full_unstemmed |
Plasmodium falciparum TryThrA antigen synthetic peptides block in vitro merozoite invasion to erythrocytes |
title_sort |
Plasmodium falciparum TryThrA antigen synthetic peptides block in vitro merozoite invasion to erythrocytes |
dc.subject.keyword.spa.fl_str_mv |
Peptides Tryptophan-threonine-rich antigen Plasmodium falciparum Malaria Invasion |
topic |
Peptides Tryptophan-threonine-rich antigen Plasmodium falciparum Malaria Invasion |
description |
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. |
publishDate |
2006 |
dc.date.created.spa.fl_str_mv |
2006-01-20 |
dc.date.accessioned.none.fl_str_mv |
2020-08-06T16:20:22Z |
dc.date.available.none.fl_str_mv |
2020-08-06T16:20:22Z |
dc.type.eng.fl_str_mv |
article |
dc.type.coarversion.fl_str_mv |
http://purl.org/coar/version/c_970fb48d4fbd8a85 |
dc.type.coar.fl_str_mv |
http://purl.org/coar/resource_type/c_6501 |
dc.type.spa.spa.fl_str_mv |
Artículo |
dc.identifier.doi.none.fl_str_mv |
https://doi.org/10.1016/j.bbrc.2005.11.089 |
dc.identifier.issn.none.fl_str_mv |
ISSN: 0006-291X EISSN: 1090-2104 |
dc.identifier.uri.none.fl_str_mv |
https://repository.urosario.edu.co/handle/10336/25978 |
url |
https://doi.org/10.1016/j.bbrc.2005.11.089 https://repository.urosario.edu.co/handle/10336/25978 |
identifier_str_mv |
ISSN: 0006-291X EISSN: 1090-2104 |
dc.language.iso.spa.fl_str_mv |
eng |
language |
eng |
dc.relation.citationEndPage.none.fl_str_mv |
896 |
dc.relation.citationIssue.none.fl_str_mv |
No. 3 |
dc.relation.citationStartPage.none.fl_str_mv |
888 |
dc.relation.citationTitle.none.fl_str_mv |
Biochemical and Biophysical Research Communications |
dc.relation.citationVolume.none.fl_str_mv |
Vol. 339 |
dc.relation.ispartof.spa.fl_str_mv |
Biochemical and Biophysical Research Communications, ISSN: 0006-291X;EISSN: 1090-2104, Vol.339, No.3 (2006); pp.888-896 |
dc.relation.uri.spa.fl_str_mv |
https://www.sciencedirect.com/science/article/abs/pii/S0006291X05026240 |
dc.rights.coar.fl_str_mv |
http://purl.org/coar/access_right/c_16ec |
dc.rights.acceso.spa.fl_str_mv |
Restringido (Acceso a grupos específicos) |
rights_invalid_str_mv |
Restringido (Acceso a grupos específicos) http://purl.org/coar/access_right/c_16ec |
dc.format.mimetype.none.fl_str_mv |
application/pdf |
dc.publisher.spa.fl_str_mv |
Elsevier |
dc.source.spa.fl_str_mv |
Biochemical and Biophysical Research Communications |
institution |
Universidad del Rosario |
dc.source.instname.none.fl_str_mv |
instname:Universidad del Rosario |
dc.source.reponame.none.fl_str_mv |
reponame:Repositorio Institucional EdocUR |
repository.name.fl_str_mv |
Repositorio institucional EdocUR |
repository.mail.fl_str_mv |
edocur@urosario.edu.co |
_version_ |
1808390982770622464 |