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                <text>&lt;strong&gt;Characterisation of Antigen B Protein Species Present in the Hydatid Cyst Fluid of Echinococcus canadensis G7 Genotype&lt;/strong&gt;</text>
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                <text>The larva of cestodes belonging to the Echinococcus granulosus sensu lato (s.l.) complex causes cystic echinococcosis (CE). It is a globally distributed zoonosis with significant economic and public health impact. The most immunogenic and specific Echinococcus-genus antigen for human CE diagnosis is antigen B (AgB), an abundant lipoprotein of the hydatid cyst fluid (HF). The AgB protein moiety (apolipoprotein) is encoded by five genes (AgB1-AgB5), which generate mature 8 kDa proteins (AgB8/1-AgB8/5). These genes seem to be differentially expressed among Echinococcus species. Since AgB immunogenicity lies on its protein moiety, differences in AgB expression within E. granulosus s.l. complex might have diagnostic and epidemiological relevance for discriminating the contribution of distinct species to human CE. Interestingly, AgB2 was proposed as a pseudogene in E. canadensis, which is the second most common cause of human CE, but proteomic studies for verifying it have not been performed yet. Herein, we analysed the protein and lipid composition of AgB obtained from fertile HF of swine origin (E. canadensis G7 genotype). AgB apolipoproteins were identified and quantified using mass spectrometry tools. Results showed that AgB8/1 was the major protein component, representing 71% of total AgB apolipoproteins, followed by AgB8/4 (15.5%), AgB8/3 (13.2%) and AgB8/5 (0.3%). AgB8/2 was not detected. As a methodological control, a parallel analysis detected all AgB apolipoproteins in bovine fertile HF (G1/3/5 genotypes). Overall, E. canadensis AgB comprised mostly AgB8/1 together with a heterogeneous mixture of lipids, and AgB8/2 was not detected despite using high sensitivity proteomic techniques. This endorses genomic data supporting that AgB2 behaves as a pseudogene in G7 genotype. Since recombinant AgB8/2 has been found to be diagnostically valuable for human CE, our findings indicate that its use as antigen in immunoassays could contribute to false negative results in areas where E. canadensis circulates. Furthermore, the presence of anti-AgB8/2 antibodies in serum may represent a useful parameter to rule out E. canadensis infection when human CE is diagnosed.</text>
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                <text>&lt;strong&gt;Folle, Ana Maite&lt;/strong&gt;</text>
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                <text>PLOS Neglected Tropical Diseases |g v. 11, no. 1, 2017. -- 17p.--e0005250</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>DOI: 10.1371/journal.pntd.0005250</text>
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                <text>&lt;strong&gt;Echinococcus granulosus Antigen B binds to monocytes and macrophages modulating cell response to inflammation&lt;/strong&gt;</text>
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                <text>ECHINOCOCCUS GRANULOSUS</text>
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                <text>ANTIGENO B</text>
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                <text>Antigen B (EgAgB) is an abundant lipoprotein released by the larva of the cestode Echinococcus granulosus into the host tissues. Its protein moiety belongs to the cestode-specific family known as hydrophobic ligand binding protein (HLBP), and is encoded by five gene subfamilies (EgAgB8/1-EgAgB8/5). The functions of EgAgB in parasite biology remain unclear. It may play a role in the parasite&amp;rsquo;s lipid metabolism since it carries host lipids that E. granulosus is unable to synthesise. On the other hand, there is evidence supporting immuno-modulating activities in EgAgB, particularly on innate immune cells. Both hypothetical functions might involve EgAgB interactions with monocytes and macrophages, which have not been formally analysed yet.</text>
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                <text>&lt;strong&gt;Silva-Alvarez, Valeria&lt;/strong&gt;</text>
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                <text>Parasites and Vectors&amp;nbsp; v. 9, no. 1, 2016.-- 17p.--e69</text>
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                <text>BioMed Central</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>PLoS Neglected Tropical Diseases v. 9, no. 3, 2015. --e0003552, 23</text>
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                <text>Echinococcus granulosus;antigen B;MoAbs;epitope mapping;repetitive epitopes The present work describes the purification and characterization of antigen B (AgB), the thermostable lipoprotein from E. granulosus. Native AgB was purified to homogeneity by a new strategy involving adsorption on DEAE-Sepharose, followed by immunopurification. The purified antigen was analysed using mapped monoclonal antibodies (MoAbs) and peptide isolation by in situ digestion in gels after SDS-PAGE. Epitope mapping of 7 MoAbs using PEPSCAN, synthetic peptides and competition studies, revealed that six of them defined epitopes which clustered the N-terminal extension of a 8 kDa subunit of AgB, whilst the remaining one reacted against the stretch RGLIAEGE, corresponding to the C-terminus. The epitopes defined by the seven MoAbs were found to be present in all the subunits. Furthermore, the similarities of the peptide finger prints obtained by HPLC analysis and amino acid sequencing of tryptic peptides isolated from the 8, 16 and 24 kDa subunits, indicated that they have most if not all the amino acid sequence in common. We also found evidence that the band representing a component of an apparent molecular weight of 8 kDa in SDS-PAGE, believed to be the smallest subunit of AgB, contained at least two components, which may constitute the building blocks of the higher molecular weight subunits.</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&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&lt;/p&gt;&#13;
&lt;p&gt;(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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&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&lt;/p&gt;&#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>A synthetic peptide (GU4) derived from an antigen B (AgB) subunit was serologically compared with crude antigen (HCFA); immunopurified AgB and antigen 5 (Ag5), and two other synthetic peptides, for diagnosis of human cystic hydatidosis. GU4 was derived from the sequence of AgB/2, the novel AgB subunit described by us. The other two peptides: 65 (AgB mimotope) and 89-122 (Ag5 mimotope), were described by others. Antigens B and 5 showed higher diagnostic sensitivity than corresponding peptides. All sera reacting with peptides 89-122 and GU4 also reacted with 65. The latter provided three to four times higher sensitivity than the former two peptides, but 30% lower specificity. The diagnostic efficiency of AgB (82%) was higher than those of Ag5 (74%) and HCFA (71%). Interestingly, 89-122 only reacted with hydatid sera, some of which did not react with AgB. Considering positive those reacting with 89-122 or AgB, sensitivity increases from 77% (with AgB) to 82% (combined), while specificity is the same as with AgB (86%). Our results suggest that hydatid serology may be improved by: a) combining several defined antigens (including synthetic peptides), b) design of new E. granulosus-specific mimotopes, which react with the false negative sera (16/90; 18%).</text>
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                <text>&lt;strong&gt;Barbieri, M&lt;/strong&gt;</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&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&lt;/p&gt;&#13;
&lt;p&gt;(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;&#13;
&lt;p&gt;&amp;nbsp;&lt;/p&gt;</text>
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