Insights into the structure of Triatoma Virus (TrV) capsid. Combining crystallography data with computational simulations

JUAN FRANCISCO VISO; FERNANDO ZAMARREÑO; MARÍA J. AMUNDARAIN; DIEGO M.A. GUÉRIN; MARCELO D. COSTABEL

Campinas

Encuentro; Latin American Summit Meeting on Biological Crystallography and Complementary Methods.; 2014

IUCr-UNESCO

Triatoma Virus (TrV) is an insect virus that belongs to the Dicistroviridae family and infects severalspecies of triatomine insects which are the vectors for human trypanosomiasis, commonly known asChagas disease. Because of this, TrV is proposed as a biological control against these vectors.The crystal structure of TrV was solved recently[1], but an omitted map of the structure, in the region ofthe icosahedral 5-fold axis of the capsid, shows an interesting electronic density.In this work we study the 5-fold symmetry axis of the icosahedral capsid of TrV, because it may beresponsible for the interaction between the interior and the exterior of the virus capsid, across aputative pore. Using molecular dynamics simulations, we have observed that the pore formed in this axisremains without water molecules in the region surrounded by a ring of Valines which creates a supposedhydrophobic gate. Also, we have found certain conditions where the axis is completely full of watermolecules, even in the hydrophobic region. The complete hydration of the channel may lead to its?opening?, and the interaction between the interior and the exterior of the capsid.