Junin virus entry in cells that express hDC-SIGN

FORLENZA, M. B.; ROLDAN, J. S.; MARTINEZ, M. G.; CORDO, S. M.; CANDURRA, N. A.

Rodario

Congreso; L Reunion SAIB; 2014

Virus entry and disemination can be mediated by c-type lectines as DC-SIGN, wich is a member of a family of receptor that recognizes carbohidrates structures. The main goal of this study is to provide more evidence of the interaction between human DC-SIGN and Junin virus (JUNV), wich has higly glicosilated proteins and determine the rol of cytoskeleton in the entry pathway. NHI3T3 and NIH3T3 h-DC-SIGN cells were infected in presence or absence of EGTA or the carbohydrate binding agent Griffithsin (GRFT). Both compounds inhibited nucleoprotein expression and viral yield in cultures that express the human lectin. We showed in previous work that JUNV DC-SIGN-mediated entry depends on clathrin and cholesterol. As many entry pathways are dependant of cell cytoskeleton, we studied the rol of microfilaments and microtubules during early virus infection. Inhibition of nucleoproteins expression and viral yield were observed when cells were pretreated adn infected in the presence of latrunculin A wich disrupt cortical and cytoplasmatic microfilament. In contrast, cytochalasin D, that affects cytoplasmic microfilaments or drugs that depolymerize microtubules did not show effect on JUNV multiplication or nucleoprotein expression. Taken together our results demostrate that JUNV interacts with hDC-SIGN and that JUNV.