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                <text>&lt;strong&gt;Improved immunodiagnosis of Cystic Hydatid disease by using a peptide with higher diagnostic value than that of its parent protein : echinococcus granulosus antigen B&lt;/strong&gt;</text>
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                <text>The assays are used for the diagnosis of hydatid disease are still imperfect. The reported diagnostic sensitivity and specificity vary greatly depending on the panel of sera used, the laboratory conducting the assay, and, more critically, the antigen used. To contribute to its standardization, we have recently ranked the diagnostic performances of the major parasite antigens and the available synthetic peptides using a large collection of serum samples. That work showed that antigen B (AgB) possesses the highest diagnostic value among these antigens. In the present work we further dissected its antigenicity by analyzing the reactivity of the same panel of sera against a set of synthetic peptides spanning the sequence of both AgB subunits. The N-terminal extension of these subunits appeared to be immunodominant in human infections. A 38-mer peptide (p176) delineated from the N-terminal extension of the AgB/1 subunit performed in an enzyme-linked immunosorbent assay with a higher diagnostic sensitivity (80%) and specificity (94%) than native AgB, Ag5, or any other peptide antigen tested against this collection of serum samples. In view of its high diagnostic value and its nature as a well-defined reproducible antigen, p176 could conveniently be used as a reference standard antigen in the diagnosis of hydatid disease.</text>
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                <text>Journal of Clinical Microbiology v. 38, no. 11, 2000. -- p. 3979</text>
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                <text>American Society for Microbiology</text>
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                <text>&lt;p&gt;&lt;strong&gt;Informaci&amp;oacute;n sobre Derechos de Autor&lt;/strong&gt;&lt;/p&gt;&#13;
&lt;p&gt;(Por favor lea este aviso antes de abrir los documentos u objetos)&lt;/p&gt;&#13;
&lt;p&gt;&lt;strong&gt; La legislaci&amp;oacute;n uruguaya protege el derecho&lt;/strong&gt; de autor sobre toda creaci&amp;oacute;n literaria, cient&amp;iacute;fica o art&amp;iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&amp;oacute;n a lo establecido por el derecho com&amp;uacute;n y las siguientes leyes (LEY 9.739 DE 17 DE DICIEMBRE DE 1937 SOBRE PROPIEDAD LITERARIA Y ARTISTICA CON LAS MODIFICACIONES INTRODUCIDAS POR LA LEY DE DERECHO DE AUTOR Y DERECHOS CONEXOS No. 17.616 DE 10 DE ENERO DE 2003, LEY 17.805 DE 26 DE AGOSTO DE 2004, LEY 18.046 DE 24 DE OCTUBRE DE 2006 LEY 18.046 DE 24 DE OCTUBRE DE 2006)&lt;/p&gt;&#13;
&lt;p&gt;&lt;strong&gt;ADVERTENCIA -&lt;/strong&gt; La consulta de este documento queda condicionada a la aceptaci&amp;oacute;n de las siguientes condiciones de uso: Este documento es &amp;uacute;nicamente para usos privados enmarcados en actividades de investigaci&amp;oacute;n y docencia. No se autoriza su reproducci&amp;oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&amp;oacute;n o cita de partes debe indicarse el nombre de la persona autora.&lt;/p&gt;</text>
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                <text>ISSN 0095-1137</text>
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                <text>&lt;strong&gt;The Enzymatic and Structural Basis for Inhibition of Echinococcus granulosus Thioredoxin Glutathione Reductase by Gold(I)&lt;/strong&gt;</text>
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                <text>ECHINOCOCCUS GRANULOSUS</text>
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                <text>Aims: New drugs are needed to treat flatworm infections that cause severe human diseases such as schistosomiasis. The unique flatworm enzyme thioredoxin glutathione reductase (TGR), structurally different from the human enzyme, is a key drug target. Structural studies of the flatworm Echinococcus granulosus TGR, free and complexed with AuI-MPO, a novel gold inhibitor, together with inhibition assays were performed. Results: AuI-MPO is a potent TGR inhibitor that achieves 75% inhibition at a 1:1 TGR:Au ratio and efficiently kills E. granulosus in vitro. The structures revealed salient insights: (i) unique monomer&amp;ndash;monomer interactions, (ii) distinct binding sites for thioredoxin and the glutaredoxin (Grx) domain, (iii) a single glutathione disulfide reduction site in the Grx domain, (iv) rotation of the Grx domain toward the Sec-containing redox active site, and (v) a single gold atom bound to Cys519 and Cys573 in the AuI-TGR complex. Structural modeling suggests that these residues are involved in the stabilization of the Sec-containing C-terminus. Consistently, Cys&amp;rarr;Ser mutations in these residues decreased TGR activities. Mass spectroscopy confirmed these cysteines are the primary binding site. Innovation: The identification of a primary site for gold binding and the structural model provide a basis for gold compound optimization through scaffold adjustments. Conclusions: The structural study revealed that TGR functions are achieved not only through a mobile Sec-containing redox center but also by rotation of the Grx domain and distinct binding sites for Grx domain and thioredoxin. The conserved Cys519 and Cys573 residues targeted by gold assist catalysis through stabilization of the Sec-containing redox center. Antioxid. Redox Signal. 27, 1491&amp;ndash;1504.</text>
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                <text>Antioxidants &amp;amp; Redox Signaling v. 27, no. 18, 2017. -- p. 1491-1504</text>
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                <text>Mary Ann Liebert, Inc</text>
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                <text>&lt;p&gt;&lt;strong&gt;Informaci&amp;oacute;n sobre Derechos de Autor&lt;/strong&gt;&lt;/p&gt;&#13;
&lt;p&gt;(Por favor lea este aviso antes de abrir los documentos u objetos)&lt;/p&gt;&#13;
&lt;p&gt;&lt;strong&gt; La legislaci&amp;oacute;n uruguaya protege el derecho&lt;/strong&gt; de autor sobre toda creaci&amp;oacute;n literaria, cient&amp;iacute;fica o art&amp;iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&amp;oacute;n a lo establecido por el derecho com&amp;uacute;n y las siguientes leyes (LEY 9.739 DE 17 DE DICIEMBRE DE 1937 SOBRE PROPIEDAD LITERARIA Y ARTISTICA CON LAS MODIFICACIONES INTRODUCIDAS POR LA LEY DE DERECHO DE AUTOR Y DERECHOS CONEXOS No. 17.616 DE 10 DE ENERO DE 2003, LEY 17.805 DE 26 DE AGOSTO DE 2004, LEY 18.046 DE 24 DE OCTUBRE DE 2006)&lt;/p&gt;&#13;
&lt;p&gt;&lt;strong&gt;ADVERTENCIA -&lt;/strong&gt; La consulta de este documento queda condicionada a la aceptaci&amp;oacute;n de las siguientes condiciones de uso: Este documento es &amp;uacute;nicamente para usos privados enmarcados en actividades de investigaci&amp;oacute;n y docencia. No se autoriza su reproducci&amp;oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&amp;oacute;n o cita de partes debe indicarse el nombre de la persona autora.&lt;/p&gt;</text>
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                <text>Reactive oxygen species (ROS) are an inescapable consequence of and geographical regions (Lymbery and Thompson 1988). We have aerobic metabolism: the sequential reduction of oxygen to water pro- started to characterize the antioxidant enzymes of E. granulosus, the duces superoxide radical and hydrogen peroxide. These species may causative agent of hydatid disease. While thioredoxin peroxidase may have potentially deleterious effects, since they can interact with each be the main hydrogen peroxide-metabolizing enzyme of this organism other and with cellular components, leading to radical chain reactions (Salinas et al. 1998), the results presented in this article suggest that and ultimately to cell death. Antioxidant enzymes constitute a natural regulatory system which has evolved to enable aerobic organisms to CuZnSOD activity is developmentally regulated in E. granulosus and employ oxidative metabolismwhile being protected fromthe damaging actively secreted by protoscoleces. effects of its by-products (Halliwell and Gutteridge 1999). Parasitic All E. granulosus extracts assayed possessed CuZnSOD activity organisms have an additional requirement for these enzymes, since (Table I), which was highest in protoscoleces (PSC). MnSOD activity they may also be exposed to oxidizing agents derived fromhost effector was detected only in PSC and prepatent adult worm extracts, constitutcells (Callahan et al. 1988; LoVerde 1998; Selkirk et al. 1998). It is ing less than 15% of the total SOD activity in either case. The specific thought that they have adapted to this stress by synthesizing high activity in PSC E/S products was about five times greater than that of levels of antioxidant enzymes and expressing them at the host&amp;ndash;parasite the extract, suggesting that CuZnSOD is actively secreted in vitro by interface; for instance, several variants of helminth antioxidant enzymes PSC. Low levels of CuZnSOD activity were detected in hydatid fluid are localized to the tegument or the cuticle and are released into their (HF), indicative of in vivo secretion of the enzyme, and in hydatid immediate environment (Cookson et al. 1992; Tang et al. 1995; Mei</text>
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&lt;p&gt;&lt;strong&gt; ADVERTENCIA -&lt;/strong&gt; La consulta de este documento queda condicionada a la aceptaci&amp;oacute;n de las siguientes condiciones de uso: Este documento es &amp;uacute;nicamente para usos privados enmarcados en actividades de investigaci&amp;oacute;n y docencia. No se autoriza su reproducci&amp;oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&amp;oacute;n o cita de partes debe indicarse el nombre de la persona autora.&lt;/p&gt;</text>
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                <text>EI sistema tiorredoxina (tiorredoxina: Trx y tiorredoxina reductasa: TR), mantiene la homeostasis redox de la celula acoplando el poder reductor del NADPH al intercambio reversible tiol-disulfuro. Este sistema puede reducir enzimas del tipo sustrato reductasas, que forman puentes disulfuro como parte de su cicio cata/itico, ademas de reducir puentes disulfuro formados espontaneamente. En organism os parasitos esta cascada podria operar, adem as, como defensa frente al estres oxidativo impuesto por las celulas del sistema inmune del hospedador. Hasta ahora no ha sido descrito el sistema tiorredoxina en parasitos helmintos. &#13;
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Por otra parte, durante el trabajo de esta tesis se produjeron en forma recombinante la T rx y la tiorredoxina peroxidasa (TPx) de E. granulosus,. La TPx es una peroxido de hidrogeno reductasa cuyo sitio activo es regenerado por el sistema tiorredoxina. Ambas proteinas recombinantes resultaron activas. La actividad de la TPx de proteccion del ADN ante las oxidaciones catalizadas por metales resulto potenciada en presencia de la Trx. &#13;
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Los resultados de esta tesis se discuten en el contexto del posible papel del sistema tiorredoxina y la TPx, uno de sus blancos. en la defensa de E. granulosus frente al estres oxidativo. &#13;
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&lt;p&gt;&lt;strong&gt;ADVERTENCIA -&lt;/strong&gt; La consulta de este documento queda condicionada a la aceptaci&amp;oacute;n de las siguientes condiciones de uso: Este documento es &amp;uacute;nicamente para usos privados enmarcados en actividades de investigaci&amp;oacute;n y docencia. No se autoriza su reproducci&amp;oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&amp;oacute;n o cita de partes debe indicarse el nombre de la persona autora.&lt;/p&gt;</text>
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                <text>The 14-3-3 protein, already described in the metacestode of Echinococcus multilocularis, has been characterized in the Echinococcus granulosus adult worm. Immunolocalization studies show the presence of the 14-3-3 protein in the periphery of testes and externally associated with the apical rostellum and adjacent worm tegument. The alcian blue staining in consecutive parasite sections gave similar reactivity patterns, suggesting that the 14-3-3 protein is produced and secreted by rostellar glands. Immunoblot analysis showed the presence of the 14-3-3 protein in somatic and excretory-secretory worm products with higher and smaller apparent molecular masses, respectively, than those detected in E. multilocularis or E. granulosus metacestode tissues. Conversely, the 14-3-3 protein was not detected in metacestode secretory products. Detection of anti-E. granulosus 14-3-3 reactivity in sera of experimentally infected dogs was achieved at early stages of infection. Specific antibody titres decreased during the course of infection. The possible origin and functions of the 14-3-3 protein produced by the adult worm are discussed.</text>
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                <text>Parasite Immunology v. 22, , 2000. -- p. 521-528</text>
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&lt;p&gt;(Por favor lea este aviso antes de abrir los documentos u objetos)&lt;/p&gt;&#13;
&lt;p&gt;&lt;strong&gt; La legislaci&amp;oacute;n uruguaya protege el derecho&lt;/strong&gt; de autor sobre toda creaci&amp;oacute;n literaria, cient&amp;iacute;fica o art&amp;iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&amp;oacute;n a lo establecido por el derecho com&amp;uacute;n y las siguientes leyes (LEY 9.739 DE 17 DE DICIEMBRE DE 1937 SOBRE PROPIEDAD LITERARIA Y ARTISTICA CON LAS MODIFICACIONES INTRODUCIDAS POR LA LEY DE DERECHO DE AUTOR Y DERECHOS CONEXOS No. 17.616 DE 10 DE ENERO DE 2003, LEY 17.805 DE 26 DE AGOSTO DE 2004, LEY 18.046 DE 24 DE OCTUBRE DE 2006 LEY 18.046 DE 24 DE OCTUBRE DE 2006)&lt;/p&gt;&#13;
&lt;p&gt;&lt;strong&gt; ADVERTENCIA -&lt;/strong&gt; La consulta de este documento queda condicionada a la aceptaci&amp;oacute;n de las siguientes condiciones de uso: Este documento es &amp;uacute;nicamente para usos privados enmarcados en actividades de investigaci&amp;oacute;n y docencia. No se autoriza su reproducci&amp;oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&amp;oacute;n o cita de partes debe indicarse el nombre de la persona autora.&lt;/p&gt;</text>
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                <text>In this work the characterization of P-29, a novel 29 kDa antigen from Echinococcus granulosus is reported. E. granulosus was identified while looking for parasite antigens distinct from those present in hydatid cyst fluid. A monoclonal antibody (mAb 47H.PS) prepared against protoscolex components revealed that P-29 is localized to the tegument and rostellum of protoscoleces, and to the germinal layer of the cyst, but it is absent in hydatid cyst fluid or adult worm extracts. Several internal fragments of P-29 showed sequence identity to the amino acid sequence encoded by Eg6, a partial gene sequence reported to code for an epitope of antigen 5 (Ag5), one of the major diagnostic antigens of the parasite. We confirmed that Eg6 encodes a sub-fragment of P-29 by mapping the epitope of mAb 47H.PS, and isolating the full length P-29 cDNA. Since Eg6 had been postulated to encode a fragment of Ag5, we specifically studied the relationship of P-29 and Ag5 by: (i) examining the cross-reactivity displayed by different mAbs; (ii) comparison of their peptide finger prints; and (iii) a comparative study of their diagnostic value. Our results prove unequivocally that P-29 and Ag5 are immunologically related, but different proteins, raising several questions on the current knowledge of Ag5</text>
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                <text>Molecular and Biochemical Parasitology v. 105, , 2000. -- p. 177-184</text>
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&lt;p&gt;&lt;strong&gt;ADVERTENCIA -&lt;/strong&gt; La consulta de este documento queda condicionada a la aceptaci&amp;oacute;n de las siguientes condiciones de uso: Este documento es &amp;uacute;nicamente para usos privados enmarcados en actividades de investigaci&amp;oacute;n y docencia. No se autoriza su reproducci&amp;oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&amp;oacute;n o cita de partes debe indicarse el nombre de la persona autora.&lt;/p&gt;</text>
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                <text>&lt;strong&gt;Korc, I.&lt;/strong&gt;</text>
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                <text>&lt;p&gt;&lt;em&gt;&lt;strong&gt;Informaci&amp;oacute;n sobre Derechos de Autor&lt;/strong&gt;&lt;/em&gt;&lt;/p&gt;&#13;
&lt;p&gt;(Por favor lea este aviso antes de abrir los documentos u objetos)&lt;/p&gt;&#13;
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                <text>Antigen 5 (Ag5) is a dominant secreted component of the larval stage of Echinococcus granulosus, and is highly immunogenic in human infections. Although the diagnostic value of Ag5 has been thoroughly evaluated, there has been little progress in its molecular characterization and the understanding of its biological role. In the present study, the Ag5 gene was cloned by reverse transcription-PCR on the basis of the amino acid sequences of tryptic fragments. The nucleotide sequence indicates that Ag5 is synthesized as a single polypeptide chain that is afterwards processed into single disulphide-bridged 22 and 38 kDa subunits. Whereas the 22 kDa component contains a highly conserved glycosaminoglycan-binding motif that may help to con&amp;reg;ne Ag5 in the host tissue surrounding the parasite, the 38 kDa subunit is closely related to serine proteases of the trypsin family.</text>
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                <text>Biochemical Journal v. 369, , 2003. -- p. 191-198</text>
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                <text>Biochemical Society</text>
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                <text>&lt;p&gt;&lt;strong&gt;Informaci&amp;oacute;n sobre Derechos de Autor&lt;/strong&gt;&lt;/p&gt;&#13;
&lt;p&gt;(Por favor lea este aviso antes de abrir los documentos u objetos)&lt;/p&gt;&#13;
&lt;p&gt;&lt;strong&gt; La legislaci&amp;oacute;n uruguaya protege el derecho&lt;/strong&gt; de autor sobre toda creaci&amp;oacute;n literaria, cient&amp;iacute;fica o art&amp;iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&amp;oacute;n a lo establecido por el derecho com&amp;uacute;n y las siguientes leyes (LEY 9.739 DE 17 DE DICIEMBRE DE 1937 SOBRE PROPIEDAD LITERARIA Y ARTISTICA CON LAS MODIFICACIONES INTRODUCIDAS POR LA LEY DE DERECHO DE AUTOR Y DERECHOS CONEXOS No. 17.616 DE 10 DE ENERO DE 2003, LEY 17.805 DE 26 DE AGOSTO DE 2004, LEY 18.046 DE 24 DE OCTUBRE DE 2006 LEY 18.046 DE 24 DE OCTUBRE DE 2006)&lt;/p&gt;&#13;
&lt;p&gt;&lt;strong&gt;ADVERTENCIA -&lt;/strong&gt; La consulta de este documento queda condicionada a la aceptaci&amp;oacute;n de las siguientes condiciones de uso: Este documento es &amp;uacute;nicamente para usos privados enmarcados en actividades de investigaci&amp;oacute;n y docencia. No se autoriza su reproducci&amp;oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&amp;oacute;n o cita de partes debe indicarse el nombre de la persona autora.&lt;/p&gt;</text>
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                <text>DOI 10.1042/BJ20021402</text>
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                <text>&lt;strong&gt;Combining proteomics and bioinformatics to explore novel tegumental antigens as vaccine candidates against Echinococcus granulosus infection&lt;/strong&gt;</text>
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                <text>Echinococcus granulosus is the parasite responsible for cystic echinococcosis (CE), an important worldwide‐distributed zoonosis. New effective vaccines against CE could potentially have great economic and health benefits. Here, we describe an innovative vaccine design scheme starting from an antigenic fraction enriched in tegumental antigens from the protoscolex stage (termed PSEx) already known to induce protection against CE. We first used mass spectrometry to characterize the protein composition of PSEx followed by Gene Ontology analysis to study the potential Biological Processes, Molecular Functions, and Cellular Localizations of the identified proteins. Following, antigenicity predictions and determination of conservancy degree against other organisms were determined. Thus, nine novel proteins were identified as potential vaccine candidates. Furthermore, linear B cell epitopes free of posttranslational modifications were predicted in the whole PSEx proteome through colocalization of in silico predicted epitopes within peptide fragments identified by matrix‐assisted laser desorption/ionization‐TOF/TOF. Resulting peptides were termed &amp;ldquo;clean linear B cell epitopes,&amp;rdquo; and through BLASTp scanning against all nonhelminth proteins, those with 100% identity against any other protein were discarded. Then, the secondary structure was predicted for peptides and their corresponding proteins. Peptides with highly similar secondary structure respect to their parental protein were selected, and those potentially toxic and/or allergenic were discarded. Finally, the selected clean linear B cell epitopes were mapped within their corresponding 3D‐modeled protein to analyze their possible antibody accessibilities, resulting in 14 putative peptide vaccine candidates. We propose nine novel proteins and 14 peptides to be further tested as vaccine candidates against CE.</text>
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                <text>&lt;strong&gt;Miles, Sebasti&amp;aacute;n&lt;/strong&gt;</text>
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                <text>&lt;strong&gt;Portela, Madel&amp;oacute;n&lt;/strong&gt;</text>
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                <text>&lt;strong&gt;Cyrklaff, Marek&lt;/strong&gt;</text>
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                <text>&lt;strong&gt;Ancarola, Mar&amp;iacute;a Eugenia&lt;/strong&gt;</text>
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                <text>&lt;strong&gt;Frischknecht, Friedrich&lt;/strong&gt;</text>
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                <text>&lt;strong&gt;Dur&amp;aacute;n, Rosario&lt;/strong&gt;</text>
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                <text>&lt;a title="Curriculum Vitae" href="https://exportcvuy.anii.org.uy/CvEstatico/?urlId=086432105a0be10ef4e4e57df7e51e5a096203688a890b013ec9a12794f41c17f3cd780253064d2d2485395b80b566f9216f3b1d82011d108cd4ea1ac4e03220&amp;amp;formato=pdf&amp;amp;convocatoria=21" target="_self"&gt;&lt;strong&gt;Dematteis, Sylvia&lt;/strong&gt;&lt;/a&gt;</text>
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                <text>Journal of Cellular Biochemistry v. 120, 2019. -p. 15320-15336</text>
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                <text>&lt;p&gt;&lt;strong&gt;Informaci&amp;oacute;n sobre Derechos de Autor&lt;/strong&gt;&lt;/p&gt;&#13;
&lt;p&gt;(Por favor lea este aviso antes de abrir los documentos u objetos)&lt;/p&gt;&#13;
&lt;p&gt;&lt;strong&gt; La legislaci&amp;oacute;n uruguaya protege el derecho&lt;/strong&gt; de autor sobre toda creaci&amp;oacute;n literaria, cient&amp;iacute;fica o art&amp;iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&amp;oacute;n a lo establecido por el derecho com&amp;uacute;n y las siguientes leyes (LEY 9.739 DE 17 DE DICIEMBRE DE 1937 SOBRE PROPIEDAD LITERARIA Y ARTISTICA CON LAS MODIFICACIONES INTRODUCIDAS POR LA LEY DE DERECHO DE AUTOR Y DERECHOS CONEXOS No. 17.616 DE 10 DE ENERO DE 2003, LEY 17.805 DE 26 DE AGOSTO DE 2004, LEY 18.046 DE 24 DE OCTUBRE DE 2006)&lt;/p&gt;&#13;
&lt;p&gt;&lt;strong&gt;ADVERTENCIA -&lt;/strong&gt; La consulta de este documento queda condicionada a la aceptaci&amp;oacute;n de las siguientes condiciones de uso: Este documento es &amp;uacute;nicamente para usos privados enmarcados en actividades de investigaci&amp;oacute;n y docencia. No se autoriza su reproducci&amp;oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&amp;oacute;n o cita de partes debe indicarse el nombre de la persona autora.&lt;/p&gt;</text>
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                <text>The larval stage of the cestode Echinococcus granulosus causes cystic echinococcosis in humans and livestock. This larva is protected by the millimeter-thick, mucin-based laminated layer (LL), from which materials have to be shed to allow parasite growth. We previously reported that dendritic cells (DCs) respond to microscopic pieces of the mucin gel of the LL (pLL) with unconventional maturation phenotypes, in the absence or presence of Toll-like receptor (TLR) agonists, including lipopolysaccharide (LPS). We also reported that the presence of pLL inhibited the activating phosphorylation of the phosphatidylinositol 3-kinase (PI3K) effector Akt induced by granulocyte-macrophage colony-stimulating factor or interleukin-4. We now show that the inhibitory effect of pLL extends to LPS as a PI3K activator, and results in diminished phosphorylation of GSK3 downstream from Akt. Functionally, the inhibition of Akt and GSK3 phosphorylation are linked to the blunted upregulation of CD40, a major feature of the unconventional maturation phenotype. Paradoxically, all aspects of unconventional maturation induced by pLL depend on PI3K class I. Additional components of the phagocytic machinery are needed, but phagocytosis of pLL particles is not required. These observations hint at a DC response mechanism related to receptor-independent mechanisms proposed for certain crystalline and synthetic polymer-based particles; this would fit the previously reported lack of detection of molecular-level motifs necessary of the effects of pLL on DCs. Finally, we report that DCs exposed to pLL are able to condition DCs not exposed to the material so that these cannot upregulate CD40 in full in response to LPS.</text>
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                <text>&lt;strong&gt;Pittini, &amp;Aacute;lvaro.&lt;/strong&gt;</text>
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                <text>&lt;strong&gt;Yamila E. Mart&amp;iacute;nez Acosta&lt;/strong&gt;</text>
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                <text>&lt;strong&gt;Allen, Judith E.&lt;/strong&gt;</text>
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                <text>Infection and Immunity v. 87, no. 12, 2019. -- p. 1-19.--e00641-19</text>
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                <text>American Society for Microbiology</text>
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            <description>Information about rights held in and over the resource</description>
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              <elementText elementTextId="546235">
                <text>&lt;p&gt;&lt;strong&gt;Informaci&amp;oacute;n sobre Derechos de Autor&lt;/strong&gt;&lt;/p&gt;&#13;
&lt;p&gt;(Por favor lea este aviso antes de abrir los documentos u objetos)&lt;/p&gt;&#13;
&lt;p&gt;&lt;strong&gt;La legislaci&amp;oacute;n uruguaya&lt;/strong&gt; protege el derecho de autor sobre toda creaci&amp;oacute;n literaria, cient&amp;iacute;fica o art&amp;iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&amp;oacute;n a lo establecido por el derecho com&amp;uacute;n y las siguientes leyes (LEY 9.739 DE 17 DE DICIEMBRE DE 1937 SOBRE PROPIEDAD LITERARIA Y ARTISTICA CON LAS MODIFICACIONES INTRODUCIDAS POR LA LEY DE DERECHO DE AUTOR Y DERECHOS CONEXOS No. 17.616 DE 10 DE ENERO DE 2003, LEY 17.805 DE 26 DE AGOSTO DE 2004, LEY 18.046 DE 24 DE OCTUBRE DE 2006 LEY 18.046 DE 24 DE OCTUBRE DE 2006)&lt;/p&gt;&#13;
&lt;p&gt;&lt;strong&gt;ADVERTENCIA -&lt;/strong&gt; La consulta de este documento queda condicionada a la aceptaci&amp;oacute;n de las siguientes condiciones de uso: Este documento es &amp;uacute;nicamente para usos privados enmarcados en actividades de investigaci&amp;oacute;n y docencia. No se autoriza su reproducci&amp;oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&amp;oacute;n o cita de partes debe indicarse el nombre de la persona autora.&lt;/p&gt;</text>
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                <text>Ingl&amp;eacute;s</text>
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                <text>DOI: 10.1128/IAI.00641-19</text>
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                  <text>Bibliografía Nacional Química</text>
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                  <text>Contiene la producción científica nacional de los profesionales químicos e investigadores, durante el período 1929 hasta la fecha.</text>
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                  <text>Departamento de Documentación y Biblioteca</text>
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                <text>&lt;strong&gt;Comparative analysis of two different subunits of antigen B from E.granulosus : |b gene sequence&lt;/strong&gt;</text>
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                <text>ECHINOCOCCUS GRANULOSUS</text>
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                <text>SEROLOGIA</text>
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                <text>ESCHERICHIA COLI</text>
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                <text>BIBLIOGRAFIA NACIONAL QUIMICA</text>
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                <text>2000</text>
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                <text>Two different Echinococcus granulosus antigen B subunits (AgB8:1 and AgB8:2) were characterized and the structure of the genes encoding these two proteins were compared. DNA sequences were expressed in Escherichia coli and the antigens&amp;rsquo; diagnostic value was then assessed. The genomic sequence of AgB8:1 has a 92 bp intron in the position corresponding to amino acid 16; the AgB8:2 genomic sequence presents a 68 bp intron in the position corresponding to amino acid 20. Both introns are located between the putative N-terminal hydrophobic sequence and the secreted peptide. A comparison between the AgB8:1 and AgB8:2 nucleotide sequences showed a 53.5% identity among exons and a 50% identity between introns. According to the molecular diversity analysis, the elapsed time since both genes shared a common ancestor would be around 4.2�107 years. When the native AgB and the two recombinant antigens (rAgB8:1 and rAgB8:2) were tested in an anti-IgG ELISA, the sensitivity of the native antigen B was 77.41% and its specificity was 81.9%, while rAgB8:1 showed 54.84% of sensitivity and 80.17% of specificity and rAg138:2 had an 83.87% sensitivity and a 98.28% specificity. Statistical analysis confirms that rAgB8:2 has a better performance than rAgB8:1 and native AgB in ELISA</text>
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            <name>Creator</name>
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                <text>&lt;strong&gt;Rott, M.B&lt;/strong&gt;</text>
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                <text>&lt;a title="Curriculum Vitae" href="http://buscadores.anii.org.uy/buscador_sni/exportador/ExportarPdf?hash=df0341a1f28a6244d86ad94a750c3ec2"&gt;&lt;strong&gt;Fern&amp;aacute;ndez, V&lt;/strong&gt;&lt;/a&gt;</text>
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                <text>&lt;strong&gt;Farias, S&lt;/strong&gt;</text>
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                <text>&lt;strong&gt;Ceni, J&lt;/strong&gt;</text>
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                <text>&lt;strong&gt;Ferreira, H. B.&lt;/strong&gt;</text>
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                <text>&lt;strong&gt;Haag, K.L&lt;/strong&gt;</text>
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                <text>&lt;strong&gt;Zaha, A.&lt;/strong&gt;</text>
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            <name>Source</name>
            <description>A related resource from which the described resource is derived</description>
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                <text>Acta Tropica v. 75, , 2000. -- p. 331-340</text>
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                <text>Elsevier</text>
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            <name>Date</name>
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                <text>2000</text>
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            <name>Rights</name>
            <description>Information about rights held in and over the resource</description>
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              <elementText elementTextId="304268">
                <text>&lt;p&gt;&lt;strong&gt;Informaci&amp;oacute;n sobre Derechos de Autor&lt;/strong&gt;&lt;/p&gt;&#13;
&lt;p&gt;(Por favor lea este aviso antes de abrir los documentos u objetos)&lt;/p&gt;&#13;
&lt;p&gt;&lt;strong&gt;La legislaci&amp;oacute;n uruguaya protege el derecho&lt;/strong&gt; de autor sobre toda creaci&amp;oacute;n literaria, cient&amp;iacute;fica o art&amp;iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&amp;oacute;n a lo establecido por el derecho com&amp;uacute;n y las siguientes leyes (LEY 9.739 DE 17 DE DICIEMBRE DE 1937 SOBRE PROPIEDAD LITERARIA Y ARTISTICA CON LAS MODIFICACIONES INTRODUCIDAS POR LA LEY DE DERECHO DE AUTOR Y DERECHOS CONEXOS No. 17.616 DE 10 DE ENERO DE 2003, LEY 17.805 DE 26 DE AGOSTO DE 2004, LEY 18.046 DE 24 DE OCTUBRE DE 2006 LEY 18.046 DE 24 DE OCTUBRE DE 2006)&lt;/p&gt;&#13;
&lt;p&gt;&lt;strong&gt;ADVERTENCIA -&lt;/strong&gt; La consulta de este documento queda condicionada a la aceptaci&amp;oacute;n de las siguientes condiciones de uso: Este documento es &amp;uacute;nicamente para usos privados enmarcados en actividades de investigaci&amp;oacute;n y docencia. No se autoriza su reproducci&amp;oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&amp;oacute;n o cita de partes debe indicarse el nombre de la persona autora.&lt;/p&gt;</text>
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                <text>Ingl&amp;eacute;s</text>
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                <text>&lt;strong&gt;Inefficient and abortive classical complement pathway activation by the calcium inositol hexakisphosphate component of the Echinococcus granulosus laminated layer&lt;/strong&gt;</text>
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                <text>ENFERMEDADES PARASITARIAS</text>
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                <text>BIBLIOGRAFIA NACIONAL QUIMICA</text>
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                <text>2019</text>
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          <element elementId="87">
            <name>Abstract</name>
            <description>A summary of the resource.</description>
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                <text>Persistent extracellular tissue-dwelling pathogens face the challenge of antibody-dependent activation of the classical complement pathway (CCP). A prime example of this situation is the larva of the cestode Echinococcus granulosus sensu lato, causing cystic echinococcosis. This tissue-dwelling, bladder-like larva is bounded by a cellular layer protected by the outermost acellular &amp;ldquo;laminated layer&amp;rdquo; (LL), to which host antibodies bind. The LL is made up of a mucin meshwork and interspersed nano-deposits of calcium inositol hexakisphosphate (calcium InsP6). We previously reported that calcium InsP6 bound C1q, apparently initiating CCP activation. The present work dissects CCP activation on the LL. Most of the C1 binding activity in the LL corresponded to calcium InsP6, and this binding was enhanced by partial proteolysis of the mucin meshwork. The remaining C1 binding activity was attributable to host antibodies, which included CCP-activating IgG isotypes. Calcium InsP6 made only a weak contribution to early CCP activation on the LL, suggesting inefficient C1 complex activation as reported for other polyanions. CCP activation on calcium InsP6 gave rise to a dominant population of C3b deposited onto calcium InsP6 itself that appeared to be quickly inactivated. Apparently as a result of inefficient initiation plus C3b inactivation, calcium InsP6 made no net contribution to C5 activation. We propose that the LL protects the underlying parasite cells from CCP activation through the combined effects of inefficient permeation of C1 through the mucins and C1 retention on calcium InsP6. This mechanism does not result in C5 activation, which is known to drive parasite-damaging inflammation.</text>
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          <element elementId="39">
            <name>Creator</name>
            <description>An entity primarily responsible for making the resource</description>
            <elementTextContainer>
              <elementText elementTextId="533002">
                <text>&lt;strong&gt;Barrios, Anabella A.&lt;/strong&gt;</text>
              </elementText>
              <elementText elementTextId="533003">
                <text>&lt;strong&gt;Grezzi, Leticia&lt;/strong&gt;</text>
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              <elementText elementTextId="533004">
                <text>&lt;strong&gt;Miles, Sebasti&amp;aacute;n&lt;/strong&gt;</text>
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              <elementText elementTextId="533005">
                <text>&lt;strong&gt;Mariconti, Mara&lt;/strong&gt;</text>
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              <elementText elementTextId="533006">
                <text>&lt;a title="Curriculum Vitae" href="https://exportcvuy.anii.org.uy/CvEstatico/?urlId=8077d6141c1946a30df792835b6b6ef857fe8ef0419315625ad1c8238bb9aca6cff0e2e3a0117a509b98df7dc5fd1db6728b0697ffb3f71b1ca9ceb5260c5454&amp;amp;formato=pdf&amp;amp;convocatoria=21" target="_self"&gt;&lt;strong&gt;Mourglia Ettlin, Gustavo Daniel.&lt;/strong&gt;&lt;/a&gt;</text>
              </elementText>
              <elementText elementTextId="533007">
                <text>&lt;strong&gt;Seoane, Paula I.&lt;/strong&gt;</text>
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              <elementText elementTextId="533008">
                <text>&lt;a title="Curriculum Vitae" href="https://www.google.com/url?sa=t&amp;amp;rct=j&amp;amp;q=&amp;amp;esrc=s&amp;amp;source=web&amp;amp;cd=1&amp;amp;cad=rja&amp;amp;uact=8&amp;amp;ved=2ahUKEwiR-faO27_mAhUAGrkGHbG5AxwQFjAAegQIBBAH&amp;amp;url=https%3A%2F%2Fexportcvuy.anii.org.uy%2Fpdf%2F%3Fc855a45b7dae1af50c961a96b5eb15c26a7b943e53f84d972caa0f9ce21ec5f03ef21e57ce461b5656b60c7a13dbc71dbc1dad52a109e231d5b638ac5639067d&amp;amp;usg=AOvVaw2-p60bssNmxkcYsJPe3H-P" target="_self"&gt;&lt;strong&gt;Alvaro, D&amp;iacute;az&lt;/strong&gt;&lt;/a&gt;</text>
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          </element>
          <element elementId="48">
            <name>Source</name>
            <description>A related resource from which the described resource is derived</description>
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              <elementText elementTextId="533009">
                <text>Immunobiology v.224, no.5, 2019. -- p. 710-719</text>
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          <element elementId="45">
            <name>Publisher</name>
            <description>An entity responsible for making the resource available</description>
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              <elementText elementTextId="533010">
                <text>Elsevier</text>
              </elementText>
            </elementTextContainer>
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          <element elementId="40">
            <name>Date</name>
            <description>A point or period of time associated with an event in the lifecycle of the resource</description>
            <elementTextContainer>
              <elementText elementTextId="533011">
                <text>2019</text>
              </elementText>
            </elementTextContainer>
          </element>
          <element elementId="47">
            <name>Rights</name>
            <description>Information about rights held in and over the resource</description>
            <elementTextContainer>
              <elementText elementTextId="533012">
                <text>&lt;p&gt;&lt;strong&gt;Informaci&amp;oacute;n sobre Derechos de Autor&lt;/strong&gt;&lt;/p&gt;&#13;
&lt;p&gt;(Por favor lea este aviso antes de abrir los documentos u objetos)&lt;/p&gt;&#13;
&lt;p&gt;&lt;strong&gt;La legislaci&amp;oacute;n uruguaya protege el derecho&lt;/strong&gt; de autor sobre toda creaci&amp;oacute;n literaria, cient&amp;iacute;fica o art&amp;iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&amp;oacute;n a lo establecido por el derecho com&amp;uacute;n y las siguientes leyes (LEY 9.739 DE 17 DE DICIEMBRE DE 1937 SOBRE PROPIEDAD LITERARIA Y ARTISTICA CON LAS MODIFICACIONES INTRODUCIDAS POR LA LEY DE DERECHO DE AUTOR Y DERECHOS CONEXOS No. 17.616 DE 10 DE ENERO DE 2003, LEY 17.805 DE 26 DE AGOSTO DE 2004, LEY 18.046 DE 24 DE OCTUBRE DE 2006)&lt;/p&gt;&#13;
&lt;p&gt;&lt;strong&gt;ADVERTENCIA -&lt;/strong&gt; La consulta de este documento queda condicionada a la aceptaci&amp;oacute;n de las siguientes condiciones de uso: Este documento es &amp;uacute;nicamente para usos privados enmarcados en actividades de investigaci&amp;oacute;n y docencia. No se autoriza su reproducci&amp;oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&amp;oacute;n o cita de partes debe indicarse el nombre de la persona autora.&lt;/p&gt;</text>
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          <element elementId="42">
            <name>Format</name>
            <description>The file format, physical medium, or dimensions of the resource</description>
            <elementTextContainer>
              <elementText elementTextId="533013">
                <text>PDF</text>
              </elementText>
            </elementTextContainer>
          </element>
          <element elementId="44">
            <name>Language</name>
            <description>A language of the resource</description>
            <elementTextContainer>
              <elementText elementTextId="533014">
                <text>Inglés</text>
              </elementText>
            </elementTextContainer>
          </element>
          <element elementId="51">
            <name>Type</name>
            <description>The nature or genre of the resource</description>
            <elementTextContainer>
              <elementText elementTextId="533015">
                <text>Art&amp;iacute;culo</text>
              </elementText>
            </elementTextContainer>
          </element>
          <element elementId="43">
            <name>Identifier</name>
            <description>An unambiguous reference to the resource within a given context</description>
            <elementTextContainer>
              <elementText elementTextId="533016">
                <text>DOI:10.1016/j.imbio.2019.05.009</text>
              </elementText>
            </elementTextContainer>
          </element>
        </elementContainer>
      </elementSet>
    </elementSetContainer>
    <tagContainer>
      <tag tagId="221">
        <name>Echinococus granulosus</name>
      </tag>
      <tag tagId="352">
        <name>Enfermedades parasitarias</name>
      </tag>
      <tag tagId="6568">
        <name>Equinocosis Quistica</name>
      </tag>
    </tagContainer>
  </item>
</itemContainer>
