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...

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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
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id EDOCUR2_30a77500bc2ceda5af8bee1f5f01b3bd
oai_identifier_str oai:repository.urosario.edu.co:10336/26936
network_acronym_str EDOCUR2
network_name_str Repositorio EdocUR - U. Rosario
repository_id_str
spelling 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
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