<?xml version="1.0" encoding="ISO-8859-1"?><article xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance">
<front>
<journal-meta>
<journal-id>1025-028X</journal-id>
<journal-title><![CDATA[Vaccimonitor]]></journal-title>
<abbrev-journal-title><![CDATA[Vaccimonitor]]></abbrev-journal-title>
<issn>1025-028X</issn>
<publisher>
<publisher-name><![CDATA[Finlay Ediciones]]></publisher-name>
</publisher>
</journal-meta>
<article-meta>
<article-id>S1025-028X2019000200068</article-id>
<title-group>
<article-title xml:lang="en"><![CDATA[Mycobacterium tuberculosis recombinant protein Rv2626c expressed in Streptomyces lividans. Physico-chemical and Immunological characterization as potential vaccine antigen]]></article-title>
<article-title xml:lang="es"><![CDATA[Proteína recombinante Rv2626c de Mycobacterium tuberculosis expresada en Streptomyces lividans. Caracterización físico-química e inmunológica como potencial antígeno vacunal]]></article-title>
</title-group>
<contrib-group>
<contrib contrib-type="author">
<name>
<surname><![CDATA[King-Batsios]]></surname>
<given-names><![CDATA[Emmanuel N.]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
<xref ref-type="aff" rid="Aaf"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Tamargo-Santos]]></surname>
<given-names><![CDATA[Beatriz]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Marrero-Trujillo]]></surname>
<given-names><![CDATA[Gretel]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Ariel-Espinosa]]></surname>
<given-names><![CDATA[Luis]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Besada]]></surname>
<given-names><![CDATA[Vladimir]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Zayas-Vignier]]></surname>
<given-names><![CDATA[Caridad]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Sierra-González]]></surname>
<given-names><![CDATA[Victoriano Gustavo]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
</contrib-group>
<aff id="Af1">
<institution><![CDATA[,Havana University Institute of Pharmacy and Foods Department of Biotechnology &amp; Immunology]]></institution>
<addr-line><![CDATA[ Havana]]></addr-line>
<country>Cuba</country>
</aff>
<aff id="Af2">
<institution><![CDATA[,Latin American School of Medical Sciences Department of Immunology ]]></institution>
<addr-line><![CDATA[ Havana]]></addr-line>
<country>Cuba</country>
</aff>
<aff id="Af3">
<institution><![CDATA[,Center for Genetic Engineering and Biotechnology Department of Proteomics, Biomedical Research Mass Spectrometry Laboratory]]></institution>
<addr-line><![CDATA[ Havana]]></addr-line>
<country>Cuba</country>
</aff>
<aff id="Af4">
<institution><![CDATA[,Finlay Institute of Vaccines Research Direction ]]></institution>
<addr-line><![CDATA[ Havana]]></addr-line>
<country>Cuba</country>
</aff>
<aff id="Af5">
<institution><![CDATA[,Biotechnological and Pharmaceutical Industries Group (BioCubaFarma)  ]]></institution>
<addr-line><![CDATA[ Havana]]></addr-line>
<country>Cuba</country>
</aff>
<pub-date pub-type="pub">
<day>00</day>
<month>08</month>
<year>2019</year>
</pub-date>
<pub-date pub-type="epub">
<day>00</day>
<month>08</month>
<year>2019</year>
</pub-date>
<volume>28</volume>
<numero>2</numero>
<fpage>68</fpage>
<lpage>79</lpage>
<copyright-statement/>
<copyright-year/>
<self-uri xlink:href="http://scielo.sld.cu/scielo.php?script=sci_arttext&amp;pid=S1025-028X2019000200068&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://scielo.sld.cu/scielo.php?script=sci_abstract&amp;pid=S1025-028X2019000200068&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://scielo.sld.cu/scielo.php?script=sci_pdf&amp;pid=S1025-028X2019000200068&amp;lng=en&amp;nrm=iso"></self-uri><abstract abstract-type="short" xml:lang="en"><p><![CDATA[ABSTRACT Mycobacterium tuberculosis (Mtb) is a leading cause of death globally. Latent tuberculosis infection threatens 1.7 billion people. Mtb latency is mediated by a group of proteins, mainly coded by the Dormancy Safety Regulator (DosR). The protein Rv2626c is the strongest regulated member of this operon. Previous results, including ours, indicate a strong potential of Rv2626c as antigen in a new multiple tuberculosis vaccine. Objectives of this study were to purify the rRv2626c protein and characterize it physico-chemically and immunologically. The purified protein migrates as a sole band after a non-reductive PAGE-silver staining. Under reductive conditions, the dimer isoform appearing at 30.9 kDa prevails over the monomer 15.6 kDa. Mass spectrometry corroborates electrophoresis results regarding dimer molecular weight, of approximately 32 kDa. Six of its digested peptides matched those of HRP-1 protein (Rv2626c) of Mtb whereas 92.1% of its amino acid sequence contains three mutations and the addition of an amino acid. With respect to native Mtb protein, 12 of the 13 main epitopes are conserved. Antigenicity was corroborated in volunteers, the antibody responses were signi&#64257;cantly higher in a number of infected tuberculosis patients in comparison to healthy Mantoux negative donors as well as in mice immunized with reference Rv2626c, while the immune identification pattern was as expected. The purified protein was able to elicit strong immune response in mice and the resulting antibodies recognized the reference Rv2626c protein. Lastly, the productive specific yield of the Streptomyces lividans strain is sustainable. Taking these results altogether, corroborates our rRv2626c as a promising candidate as antigen for new tuberculosis vaccine formulations.]]></p></abstract>
<abstract abstract-type="short" xml:lang="es"><p><![CDATA[RESUMEN Mycobacterium tuberculosis (Mtb) es una de las principales causas de muerte globalmente, la tuberculosis latente amenaza a 1,7 mil millones de personas. En combinación con el VIH-SIDA y otras enfermedades, la tuberculosis puede ser reactivada. La latencia de Mtb está mediada por un grupo de proteínas, principalmente codificadas por el Regulador de Seguridad de Latencia (DosR). La proteína Rv2626c es el miembro más fuertemente regulado de este operón. Los resultados previos, incluidos los nuestros, indican una gran potencialidad de Rv2626c como antígeno en una nueva vacuna múltiple contra la tuberculosis. Los objetivos de este estudio fueron purificar la proteína Rv2626c y caracterizarla fisicoquímica e inmunológicamente. La proteína purificada migra como una banda única después de PAGE con tinción de plata en condiciones no reductoras. En condiciones reductoras, el dímero, de 30,9 kDa, es la isoforma prevaleciente sobre el monómero, de 15,6 kDa. La espectrometría de masas corrobora el peso molecular del dímero, de aproximadamente 32 kDa. Seis de sus péptidos digeridos coincidieron con los de la proteína Rv2626c de Mtb, mientras que se confirmó coincidencia del 92,1% de su secuencia de aminoácidos, detectándose tres mutaciones y la adición de un aminoácido. Con respecto a la proteína Mtb nativa, se conservan 12 de los 13 epítopes principales. La antigenicidad se corroboró en voluntarios, las respuestas de anticuerpos fueron significativamente mayores en un número de pacientes infectados con tuberculosis en comparación con los donantes negativos de Mantoux sanos, así como en ratones inmunizados con la referencia Rv2626c, mientras que el patrón de identificación inmune fue el esperado. La proteína purificada fue capaz de provocar una fuerte respuesta inmune en ratones y los anticuerpos resultantes reconocieron la proteína de referencia Rv2626c. Por último, el rendimiento productivo específico de la cepa de Streptomyces lividans es sostenible. Tomando estos resultados en conjunto, corrobora nuestra rRv2626c como un candidato prometedor como antígeno para nuevas formulaciones de vacunas contra la tuberculosis.]]></p></abstract>
<kwd-group>
<kwd lng="en"><![CDATA[Mycobacterium tuberculosis]]></kwd>
<kwd lng="en"><![CDATA[Rv2626c recombinant protein]]></kwd>
<kwd lng="en"><![CDATA[Streptomyces lividans]]></kwd>
<kwd lng="en"><![CDATA[tuberculosis vaccine]]></kwd>
<kwd lng="es"><![CDATA[Mycobacterium tuberculosis]]></kwd>
<kwd lng="es"><![CDATA[proteína recombinante Rv2626c]]></kwd>
<kwd lng="es"><![CDATA[Streptomyces lividans]]></kwd>
<kwd lng="es"><![CDATA[vacuna antituberculosis]]></kwd>
</kwd-group>
</article-meta>
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