The glycosylphosphatidylinositol-anchored protein repertoire of Babesia bovis and its significance for erythrocyte invasion
- Autores
- Rodriguez, Anabel Elisa; Florin-Christensen, Mónica; Flores, Daniela; Echaide, Ignacio Eduardo; Suarez, Carlos Esteban; Schnittger, Leonhard
- Año de publicación
- 2014
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión aceptada
- Descripción
- Glycosylphosphatidylinositol-anchored proteins are abundant on the surface of pathogenic protozoans and might play an important role for parasite survival. In the present work, the relevance of GPI-anchored proteins for erythrocyte invasion of the cattle hemoparasite Babesia bovis was studied. We show that cleavage of GPI-anchored antigens from the merozoite parasite stage by phosphatidylinositol-specific phospholipase C abolished invasion of erythrocytes demonstrating the importance of this class of molecules for parasite propagation. In addition, the repertoire of GPI-anchored proteins of B. bovis was predicted with high fidelity by searching its genome with available web-based bioinformatic tools. Altogether 17 GPI-anchored proteins were identified, 5 of which represent the already characterized variable merozoite surface antigens (VMSAs). Fifteen of the identified GPI-anchored proteins contain 2–26 amino acid repeats indicating that they are likely involved in functions of recognition, adhesion, or transport. Repeats were found to contain an increased frequency of proline, indicative of unstructured regions; and were estimated to be 3.21 times more hydrophilic than non-repeat regions. This suggests that they might represent eminent antibody epitopes. The majority of the putative GPI-anchored antigens reported in this work have so far remained unnoticed, though they may represent potential candidates for inclusion in a subunit vaccine.
Fil: Rodriguez, Anabel Elisa. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Patobiología; Argentina
Fil: Florin-Christensen, Monica. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Patobiología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Flores, Daniela. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Patobiología; Argentina. ANPCyT; Argentina
Fil: Echaide, Ignacio Eduardo. Instituto Nacional de Tecnología Agropecuaria (INTA). Estación Experimental Agropecuaria Rafaela; Argentina
Fil: Suarez, Carlos Esteban. Washington State University. Department of Veterinary Microbiology and Pathology; Estados Unidos
Fil: Schnittger, Leonhard. . Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Patobiología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina - Fuente
- Ticks and tick-borne diseases 5 (3) : 343-348. (April 2014)
- Materia
-
Babesia Bovis
Eritrocitos
Erythrocytes
Babesiosis
Glycosylphosphatidylinositol - Nivel de accesibilidad
- acceso restringido
- Condiciones de uso
- Repositorio
- Institución
- Instituto Nacional de Tecnología Agropecuaria
- OAI Identificador
- oai:localhost:20.500.12123/1755
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The glycosylphosphatidylinositol-anchored protein repertoire of Babesia bovis and its significance for erythrocyte invasionRodriguez, Anabel ElisaFlorin-Christensen, MónicaFlores, DanielaEchaide, Ignacio EduardoSuarez, Carlos EstebanSchnittger, LeonhardBabesia BovisEritrocitosErythrocytesBabesiosisGlycosylphosphatidylinositolGlycosylphosphatidylinositol-anchored proteins are abundant on the surface of pathogenic protozoans and might play an important role for parasite survival. In the present work, the relevance of GPI-anchored proteins for erythrocyte invasion of the cattle hemoparasite Babesia bovis was studied. We show that cleavage of GPI-anchored antigens from the merozoite parasite stage by phosphatidylinositol-specific phospholipase C abolished invasion of erythrocytes demonstrating the importance of this class of molecules for parasite propagation. In addition, the repertoire of GPI-anchored proteins of B. bovis was predicted with high fidelity by searching its genome with available web-based bioinformatic tools. Altogether 17 GPI-anchored proteins were identified, 5 of which represent the already characterized variable merozoite surface antigens (VMSAs). Fifteen of the identified GPI-anchored proteins contain 2–26 amino acid repeats indicating that they are likely involved in functions of recognition, adhesion, or transport. Repeats were found to contain an increased frequency of proline, indicative of unstructured regions; and were estimated to be 3.21 times more hydrophilic than non-repeat regions. This suggests that they might represent eminent antibody epitopes. The majority of the putative GPI-anchored antigens reported in this work have so far remained unnoticed, though they may represent potential candidates for inclusion in a subunit vaccine.Fil: Rodriguez, Anabel Elisa. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Patobiología; ArgentinaFil: Florin-Christensen, Monica. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Patobiología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Flores, Daniela. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Patobiología; Argentina. ANPCyT; ArgentinaFil: Echaide, Ignacio Eduardo. Instituto Nacional de Tecnología Agropecuaria (INTA). Estación Experimental Agropecuaria Rafaela; ArgentinaFil: Suarez, Carlos Esteban. Washington State University. Department of Veterinary Microbiology and Pathology; Estados UnidosFil: Schnittger, Leonhard. . Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Patobiología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina2017-11-13T13:38:21Z2017-11-13T13:38:21Z2014-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/acceptedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12123/1755https://www.sciencedirect.com/science/article/pii/S1877959X1400034X1877-959X (Print)1877-9603 (Online)https://doi.org/10.1016/j.ttbdis.2013.12.011Ticks and tick-borne diseases 5 (3) : 343-348. (April 2014)reponame:INTA Digital (INTA)instname:Instituto Nacional de Tecnología Agropecuariaenginfo:eu-repo/semantics/restrictedAccess2025-09-04T09:47:07Zoai:localhost:20.500.12123/1755instacron:INTAInstitucionalhttp://repositorio.inta.gob.ar/Organismo científico-tecnológicoNo correspondehttp://repositorio.inta.gob.ar/oai/requesttripaldi.nicolas@inta.gob.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:l2025-09-04 09:47:08.296INTA Digital (INTA) - Instituto Nacional de Tecnología Agropecuariafalse |
dc.title.none.fl_str_mv |
The glycosylphosphatidylinositol-anchored protein repertoire of Babesia bovis and its significance for erythrocyte invasion |
title |
The glycosylphosphatidylinositol-anchored protein repertoire of Babesia bovis and its significance for erythrocyte invasion |
spellingShingle |
The glycosylphosphatidylinositol-anchored protein repertoire of Babesia bovis and its significance for erythrocyte invasion Rodriguez, Anabel Elisa Babesia Bovis Eritrocitos Erythrocytes Babesiosis Glycosylphosphatidylinositol |
title_short |
The glycosylphosphatidylinositol-anchored protein repertoire of Babesia bovis and its significance for erythrocyte invasion |
title_full |
The glycosylphosphatidylinositol-anchored protein repertoire of Babesia bovis and its significance for erythrocyte invasion |
title_fullStr |
The glycosylphosphatidylinositol-anchored protein repertoire of Babesia bovis and its significance for erythrocyte invasion |
title_full_unstemmed |
The glycosylphosphatidylinositol-anchored protein repertoire of Babesia bovis and its significance for erythrocyte invasion |
title_sort |
The glycosylphosphatidylinositol-anchored protein repertoire of Babesia bovis and its significance for erythrocyte invasion |
dc.creator.none.fl_str_mv |
Rodriguez, Anabel Elisa Florin-Christensen, Mónica Flores, Daniela Echaide, Ignacio Eduardo Suarez, Carlos Esteban Schnittger, Leonhard |
author |
Rodriguez, Anabel Elisa |
author_facet |
Rodriguez, Anabel Elisa Florin-Christensen, Mónica Flores, Daniela Echaide, Ignacio Eduardo Suarez, Carlos Esteban Schnittger, Leonhard |
author_role |
author |
author2 |
Florin-Christensen, Mónica Flores, Daniela Echaide, Ignacio Eduardo Suarez, Carlos Esteban Schnittger, Leonhard |
author2_role |
author author author author author |
dc.subject.none.fl_str_mv |
Babesia Bovis Eritrocitos Erythrocytes Babesiosis Glycosylphosphatidylinositol |
topic |
Babesia Bovis Eritrocitos Erythrocytes Babesiosis Glycosylphosphatidylinositol |
dc.description.none.fl_txt_mv |
Glycosylphosphatidylinositol-anchored proteins are abundant on the surface of pathogenic protozoans and might play an important role for parasite survival. In the present work, the relevance of GPI-anchored proteins for erythrocyte invasion of the cattle hemoparasite Babesia bovis was studied. We show that cleavage of GPI-anchored antigens from the merozoite parasite stage by phosphatidylinositol-specific phospholipase C abolished invasion of erythrocytes demonstrating the importance of this class of molecules for parasite propagation. In addition, the repertoire of GPI-anchored proteins of B. bovis was predicted with high fidelity by searching its genome with available web-based bioinformatic tools. Altogether 17 GPI-anchored proteins were identified, 5 of which represent the already characterized variable merozoite surface antigens (VMSAs). Fifteen of the identified GPI-anchored proteins contain 2–26 amino acid repeats indicating that they are likely involved in functions of recognition, adhesion, or transport. Repeats were found to contain an increased frequency of proline, indicative of unstructured regions; and were estimated to be 3.21 times more hydrophilic than non-repeat regions. This suggests that they might represent eminent antibody epitopes. The majority of the putative GPI-anchored antigens reported in this work have so far remained unnoticed, though they may represent potential candidates for inclusion in a subunit vaccine. Fil: Rodriguez, Anabel Elisa. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Patobiología; Argentina Fil: Florin-Christensen, Monica. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Patobiología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Flores, Daniela. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Patobiología; Argentina. ANPCyT; Argentina Fil: Echaide, Ignacio Eduardo. Instituto Nacional de Tecnología Agropecuaria (INTA). Estación Experimental Agropecuaria Rafaela; Argentina Fil: Suarez, Carlos Esteban. Washington State University. Department of Veterinary Microbiology and Pathology; Estados Unidos Fil: Schnittger, Leonhard. . Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Patobiología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina |
description |
Glycosylphosphatidylinositol-anchored proteins are abundant on the surface of pathogenic protozoans and might play an important role for parasite survival. In the present work, the relevance of GPI-anchored proteins for erythrocyte invasion of the cattle hemoparasite Babesia bovis was studied. We show that cleavage of GPI-anchored antigens from the merozoite parasite stage by phosphatidylinositol-specific phospholipase C abolished invasion of erythrocytes demonstrating the importance of this class of molecules for parasite propagation. In addition, the repertoire of GPI-anchored proteins of B. bovis was predicted with high fidelity by searching its genome with available web-based bioinformatic tools. Altogether 17 GPI-anchored proteins were identified, 5 of which represent the already characterized variable merozoite surface antigens (VMSAs). Fifteen of the identified GPI-anchored proteins contain 2–26 amino acid repeats indicating that they are likely involved in functions of recognition, adhesion, or transport. Repeats were found to contain an increased frequency of proline, indicative of unstructured regions; and were estimated to be 3.21 times more hydrophilic than non-repeat regions. This suggests that they might represent eminent antibody epitopes. The majority of the putative GPI-anchored antigens reported in this work have so far remained unnoticed, though they may represent potential candidates for inclusion in a subunit vaccine. |
publishDate |
2014 |
dc.date.none.fl_str_mv |
2014-04 2017-11-13T13:38:21Z 2017-11-13T13:38:21Z |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/acceptedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
acceptedVersion |
dc.identifier.none.fl_str_mv |
http://hdl.handle.net/20.500.12123/1755 https://www.sciencedirect.com/science/article/pii/S1877959X1400034X 1877-959X (Print) 1877-9603 (Online) https://doi.org/10.1016/j.ttbdis.2013.12.011 |
url |
http://hdl.handle.net/20.500.12123/1755 https://www.sciencedirect.com/science/article/pii/S1877959X1400034X https://doi.org/10.1016/j.ttbdis.2013.12.011 |
identifier_str_mv |
1877-959X (Print) 1877-9603 (Online) |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/restrictedAccess |
eu_rights_str_mv |
restrictedAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.source.none.fl_str_mv |
Ticks and tick-borne diseases 5 (3) : 343-348. (April 2014) reponame:INTA Digital (INTA) instname:Instituto Nacional de Tecnología Agropecuaria |
reponame_str |
INTA Digital (INTA) |
collection |
INTA Digital (INTA) |
instname_str |
Instituto Nacional de Tecnología Agropecuaria |
repository.name.fl_str_mv |
INTA Digital (INTA) - Instituto Nacional de Tecnología Agropecuaria |
repository.mail.fl_str_mv |
tripaldi.nicolas@inta.gob.ar |
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1842341352095875072 |
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12.623145 |