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Abstract
Meat of the South American camelids (SACs) llama and alpaca is an important source of animal protein and income for rural families in the Andes, and a product with significant growth potential for local and international markets. However, infestation with macroscopic cysts of the coccidian protozoon Sarcocystis aucheniae, a parasitosis known as SAC sarcocystosis, significantly hampers its commercialization. There are no validated methods to diagnose the [ver mas...]
dc.contributor.authorDecker Franco, Cecilia
dc.contributor.authorWieser, Sara Nathaly
dc.contributor.authorSoria, Marcelo Abel
dc.contributor.authorDe Alba, Paloma
dc.contributor.authorFlorin-Christensen, Mónica
dc.contributor.authorSchnittger, Leonhard
dc.date.accessioned2020-08-28T16:36:10Z
dc.date.available2020-08-28T16:36:10Z
dc.date.issued2020-07
dc.identifier.issn1865-1674
dc.identifier.otherhttps://doi.org/10.1111/tbed.13438
dc.identifier.urihttp://hdl.handle.net/20.500.12123/7786
dc.identifier.urihttps://onlinelibrary.wiley.com/doi/full/10.1111/tbed.13438
dc.description.abstractMeat of the South American camelids (SACs) llama and alpaca is an important source of animal protein and income for rural families in the Andes, and a product with significant growth potential for local and international markets. However, infestation with macroscopic cysts of the coccidian protozoon Sarcocystis aucheniae, a parasitosis known as SAC sarcocystosis, significantly hampers its commercialization. There are no validated methods to diagnose the presence of S. aucheniae cysts other than carcass examination. Moreover, there are no available drugs or vaccines to cure or prevent SAC sarcocystosis. Identification of relevant molecules that act at the host–pathogen interface can significantly contribute to the control of this disease. It has been shown for other pathogenic protozoa that glycosylphosphatidylinositol (GPI) is a critical molecule implicated in parasite survival and pathogenicity. This study focused on the identification of the enzymes that participate in the S. aucheniae GPI biosynthetic pathway and the repertoire of the parasite GPI‐anchored proteins (GPI‐APs). To this aim, RNA was extracted from parasite cysts and the transcriptome was sequenced and translated into amino acid sequences. The generated database was mined using sequences of well‐characterized GPI biosynthetic enzymes of Saccharomyces cerevisiae and Toxoplasma gondii. Eleven enzymes predicted to participate in the S. aucheniae GPI biosynthetic pathway were identified. On the other hand, the database was searched for proteins carrying an N‐terminal signal peptide and a single C‐terminal transmembrane region containing a GPI anchor signal. Twenty‐four GPI‐anchored peptides were identified, of which nine are likely S. aucheniae‐specific, and 15 are homologous to membrane proteins of other coccidians. Among the latter, 13 belong to the SRS domain superfamily, an extensive group of coccidian GPI‐anchored proteins that mediate parasite interaction with their host. Phylogenetic analysis showed a great degree of intra‐ and inter‐specific divergence among SRS family proteins. In vitro and in vivo experiments are needed to validate S. aucheniae GPI biosynthetic enzymes and GPI‐APs as drug targets and/or as vaccine or diagnostic antigens.eng
dc.formatapplication/pdfes_AR
dc.language.isoenges_AR
dc.publisherWileyes_AR
dc.rightsinfo:eu-repo/semantics/openAccesses_AR
dc.sourceTransboundary and Emerging Diseases 67 (Supl. 2) : 165-174 (Julio 2020)es_AR
dc.subjectSarcocystises_AR
dc.subjectImmunotherapyeng
dc.subjectInmunoterapiaes_AR
dc.subjectDiagnostic Techniqueseng
dc.subjectTécnicas de Diagnosises_AR
dc.subjectMeateng
dc.subjectCarnees_AR
dc.subjectCamelidaees_AR
dc.subjectPathogenicityeng
dc.subjectPatogenicidades_AR
dc.subjectPhylogenyeng
dc.subjectFilogeniaes_AR
dc.subject.otherSarcocystis aucheniaees_AR
dc.titleIn silico identification of immunotherapeutic and diagnostic targets in the glycosylphosphatidylinositol metabolism of the coccidian Sarcocystis aucheniaees_AR
dc.typeinfo:ar-repo/semantics/artículoes_AR
dc.typeinfo:eu-repo/semantics/articlees_AR
dc.typeinfo:eu-repo/semantics/publishedVersiones_AR
dc.description.origenInstituto de Patobiologíaes_AR
dc.description.filFil: Decker Franco, Cecilia. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Patobiología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentinaes_AR
dc.description.filFil: Wieser, Sarah Nathaly. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Patobiología; Argentinaes_AR
dc.description.filFil: Soria, Marcelo Abel. Universidad de Buenos Aires. Facultad de Agronomía. Departamento de Biología Aplicada y Alimentos. Cátedra de Microbiología Agrícola; Argentinaes_AR
dc.description.filFil: De Alba Paloma. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Patobiología; Argentinaes_AR
dc.description.filFil: Florin-Christensen, Monica. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Patobiología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentinaes_AR
dc.description.filFil: Schnittger, Leonhard. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Patobiología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentinaes_AR
dc.subtypecientifico


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