Evaluación de la actividad oxido-reductora de PDI durante la unión PDI-TLPs de rotavirus en la membrana citoplasmática de vellosidades intestinales aisladas de ratón ICR adulto
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La infectividad de rotavirus es reducida por moléculas que alteran el intercambio tiol-disulfuro y por anticuerpos contra PDI. El objetivo fue evaluar la interacción y asociación funcional entre PDI y TLPs de Rotavirus durante etapas tempranas de internalización del virus. PDI soluble, células integras o fracciones enriquecidas de membrana citoplasmática se incubaron con rotavirus en presencia o ausencia de agentes que bloquean el ambiente redox evaluando la interacción de PDI-rotavirus, PDI-proteínas virales y los cambios redox de las proteínas virales. Se evidenció interacción de PDI soluble y PDI de membrana con TLPs de rotavirus y con proteínas virales solubles. La interacción disminuye al tratamiento con agentes que bloquean el intercambio tiol-disulfuro. Incubar rotavirus con fracciones enriquecidas de membrana genera cambios en la distribución de tioles en las proteínas estructurales del virus VP7, VP6 y VP4. PDI interacciona con rotavirus y participa en los mecanismos redox que Rotavirus requiere para entrar a la célula.
Abstract. Rotavirus infection is interfered by thiol-disulfide exchange inhibitors and antibodies against PDI. The objective was to assess the physical and functional interactions between PDI and TLPs rotaviruses during the early steps of virus internalization. Accordingly, cells, cell membrane-enriched fractions or soluble PDI were incubated with rotavirus in the presence or absence of thiol-disulfide exchange inhibitors. PDI-rotavirus, PDI-isolated or recombinant viral proteins and redox changes in viral proteins were assessed. The evidence was shown for an interaction of soluble PDI or cell membrane-associated PDI with rotaviral soluble proteins or TLPs rotaviruses. These interactions were reduced with agents that block thiol-disulfide exchange. Incubation of rotavirus with cell membrane-enriched fractions affected the thiol-disulfide distribution in the structural rotavirus proteins VP4, VP6 and VP7. PDI interacts with rotavirus particles and participates in redox mechanisms that are used by rotaviruses during entry into their host cells.
Abstract. Rotavirus infection is interfered by thiol-disulfide exchange inhibitors and antibodies against PDI. The objective was to assess the physical and functional interactions between PDI and TLPs rotaviruses during the early steps of virus internalization. Accordingly, cells, cell membrane-enriched fractions or soluble PDI were incubated with rotavirus in the presence or absence of thiol-disulfide exchange inhibitors. PDI-rotavirus, PDI-isolated or recombinant viral proteins and redox changes in viral proteins were assessed. The evidence was shown for an interaction of soluble PDI or cell membrane-associated PDI with rotaviral soluble proteins or TLPs rotaviruses. These interactions were reduced with agents that block thiol-disulfide exchange. Incubation of rotavirus with cell membrane-enriched fractions affected the thiol-disulfide distribution in the structural rotavirus proteins VP4, VP6 and VP7. PDI interacts with rotavirus particles and participates in redox mechanisms that are used by rotaviruses during entry into their host cells.