Serine Repeat Antigen Peptides which bind specifically to Red Blood Cells.
It has been reported that serine repeat antigen (SERA) binds directly to human erythrocyte membranes, inside-out vesicles and intact mouse erythrocytes. Similarly, mAbs specific against SERA are effective in blocking red blood cell (RBC) invasion by P. falciparum merozoites. Furthermore, the N-termi...
- Autores:
- Tipo de recurso:
- Fecha de publicación:
- 2000
- Institución:
- Universidad del Rosario
- Repositorio:
- Repositorio EdocUR - U. Rosario
- Idioma:
- eng
- OAI Identifier:
- oai:repository.urosario.edu.co:10336/26936
- Acceso en línea:
- https://doi.org/10.1016/S1383-5769(00)00040-4
https://repository.urosario.edu.co/handle/10336/26936
- Palabra clave:
- P. falciparum
Serine repeat antigen protein
Binding peptides
Merozoite invasion
- Rights
- License
- Restringido (Acceso a grupos específicos)
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Repositorio EdocUR - U. Rosario |
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b120ef67-32d0-439e-802d-7041ce4957c1-1b8902bd8-16f9-4e10-84ce-847819e12c56-134b82e95-53e0-4ba5-a5c5-d4191164afa1-1e24a8b75-8725-433a-8f7d-b1de864249ab-1dd3af730-1a89-42fc-a5de-64665dc12a41-151721018-1dbe17748-4c0d-479b-ac09-27bf4a63b6e5-124b56de8-80c5-41dc-a81e-d0321ed4115a-12020-08-19T14:40:34Z2020-08-19T14:40:34Z2000It has been reported that serine repeat antigen (SERA) binds directly to human erythrocyte membranes, inside-out vesicles and intact mouse erythrocytes. Similarly, mAbs specific against SERA are effective in blocking red blood cell (RBC) invasion by P. falciparum merozoites. Furthermore, the N-terminal recombinant SERA fragment inhibits the merozoite invasion of erythrocyte. In this study of 49 non-overlapping 20-residue-long peptides encompassing the whole SERA protein FCR3 strain, seven peptides having high RBC binding activity were found. Six of these peptides (three from the SERA N-terminal domain) are located in conserved regions and show affinity constants between 150 and 1100 nM, Hill coefficients between 1.5 and 3.0 and 30 000–120 000 binding sites per cell. Some of these peptides inhibited in vitro merozoite invasion of erythrocyte and intra-erythrocytic development. Residues which are critical in the binding to erythrocytes (in bold face), i.e. 6725 (YLKETNNAISFESNSGSLEKK), 6733 (YALGSDIPEKCDTLASNCFLS), 6737 (YDNILVKMFKTNENNDKSELI), 6746 (DQGNCDTSWIFASKYHLETI), 6754 (YKKVQNLCGDDTADHAVNIVG) and 6762 (NEVSERVHVYHILKHIKDGK), were determined by means of competition assays with high-binding peptide glycine analogues. The identification of peptides which bind to erythrocyte membrane is important in understanding the process of RBC invasion by P. falciparum merozoites.application/pdfhttps://doi.org/10.1016/S1383-5769(00)00040-4ISSN: 1383-5769EISSN: 1873-0329https://repository.urosario.edu.co/handle/10336/26936engElsevier117No. 2105Parasitology InternationalVol. 49Parasitology International, ISSN:1383-5769; EISSN: 1873-0329, Vol.49, No.2 (1 August 2000); pp. 105-117https://www.sciencedirect.com/science/article/abs/pii/S1383576900000404Restringido (Acceso a grupos específicos)http://purl.org/coar/access_right/c_16ecParasitology Internationalinstname:Universidad del Rosarioreponame:Repositorio Institucional EdocURP. falciparumSerine repeat antigen proteinBinding peptidesMerozoite invasionSerine Repeat Antigen Peptides which bind specifically to Red Blood Cells.Péptidos de antígeno repetido de serina que se unen específicamente a los glóbulos rojos.articleArtículohttp://purl.org/coar/version/c_970fb48d4fbd8a85http://purl.org/coar/resource_type/c_6501Puentes. AGarcia, JavierVera. RicardoLopez, RamsesUrquiza, MauricioVanegas, MagnoliaSalazar, Luz MaryPatarrooyo, Manuel Elkin10336/26936oai:repository.urosario.edu.co:10336/269362021-06-03 00:50:02.572https://repository.urosario.edu.coRepositorio institucional EdocURedocur@urosario.edu.co |
dc.title.spa.fl_str_mv |
Serine Repeat Antigen Peptides which bind specifically to Red Blood Cells. |
dc.title.TranslatedTitle.spa.fl_str_mv |
Péptidos de antígeno repetido de serina que se unen específicamente a los glóbulos rojos. |
title |
Serine Repeat Antigen Peptides which bind specifically to Red Blood Cells. |
spellingShingle |
Serine Repeat Antigen Peptides which bind specifically to Red Blood Cells. P. falciparum Serine repeat antigen protein Binding peptides Merozoite invasion |
title_short |
Serine Repeat Antigen Peptides which bind specifically to Red Blood Cells. |
title_full |
Serine Repeat Antigen Peptides which bind specifically to Red Blood Cells. |
title_fullStr |
Serine Repeat Antigen Peptides which bind specifically to Red Blood Cells. |
title_full_unstemmed |
Serine Repeat Antigen Peptides which bind specifically to Red Blood Cells. |
title_sort |
Serine Repeat Antigen Peptides which bind specifically to Red Blood Cells. |
dc.subject.keyword.spa.fl_str_mv |
P. falciparum Serine repeat antigen protein Binding peptides Merozoite invasion |
topic |
P. falciparum Serine repeat antigen protein Binding peptides Merozoite invasion |
description |
It has been reported that serine repeat antigen (SERA) binds directly to human erythrocyte membranes, inside-out vesicles and intact mouse erythrocytes. Similarly, mAbs specific against SERA are effective in blocking red blood cell (RBC) invasion by P. falciparum merozoites. Furthermore, the N-terminal recombinant SERA fragment inhibits the merozoite invasion of erythrocyte. In this study of 49 non-overlapping 20-residue-long peptides encompassing the whole SERA protein FCR3 strain, seven peptides having high RBC binding activity were found. Six of these peptides (three from the SERA N-terminal domain) are located in conserved regions and show affinity constants between 150 and 1100 nM, Hill coefficients between 1.5 and 3.0 and 30 000–120 000 binding sites per cell. Some of these peptides inhibited in vitro merozoite invasion of erythrocyte and intra-erythrocytic development. Residues which are critical in the binding to erythrocytes (in bold face), i.e. 6725 (YLKETNNAISFESNSGSLEKK), 6733 (YALGSDIPEKCDTLASNCFLS), 6737 (YDNILVKMFKTNENNDKSELI), 6746 (DQGNCDTSWIFASKYHLETI), 6754 (YKKVQNLCGDDTADHAVNIVG) and 6762 (NEVSERVHVYHILKHIKDGK), were determined by means of competition assays with high-binding peptide glycine analogues. The identification of peptides which bind to erythrocyte membrane is important in understanding the process of RBC invasion by P. falciparum merozoites. |
publishDate |
2000 |
dc.date.created.spa.fl_str_mv |
2000 |
dc.date.accessioned.none.fl_str_mv |
2020-08-19T14:40:34Z |
dc.date.available.none.fl_str_mv |
2020-08-19T14:40:34Z |
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/S1383-5769(00)00040-4 |
dc.identifier.issn.none.fl_str_mv |
ISSN: 1383-5769 EISSN: 1873-0329 |
dc.identifier.uri.none.fl_str_mv |
https://repository.urosario.edu.co/handle/10336/26936 |
url |
https://doi.org/10.1016/S1383-5769(00)00040-4 https://repository.urosario.edu.co/handle/10336/26936 |
identifier_str_mv |
ISSN: 1383-5769 EISSN: 1873-0329 |
dc.language.iso.spa.fl_str_mv |
eng |
language |
eng |
dc.relation.citationEndPage.none.fl_str_mv |
117 |
dc.relation.citationIssue.none.fl_str_mv |
No. 2 |
dc.relation.citationStartPage.none.fl_str_mv |
105 |
dc.relation.citationTitle.none.fl_str_mv |
Parasitology International |
dc.relation.citationVolume.none.fl_str_mv |
Vol. 49 |
dc.relation.ispartof.spa.fl_str_mv |
Parasitology International, ISSN:1383-5769; EISSN: 1873-0329, Vol.49, No.2 (1 August 2000); pp. 105-117 |
dc.relation.uri.spa.fl_str_mv |
https://www.sciencedirect.com/science/article/abs/pii/S1383576900000404 |
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 |
Parasitology International |
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_ |
1814167486156767232 |