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

JUAN FRANCISCO VISO; FERNANDO ZAMARREÑO; MARÍA JULIA AMUNDARAIN; DIEGO M A GUÉRIN; MARCELO DANIEL COSTABEL

Campinas

Congreso; IYCr2014 - Latin american summit meeting on biological crystallography and complementary methods; 2014

Triatoma Virus (TrV) is an insect virus that belongs to the Dicistroviridae family and infects several species of triatomine insects which are the vectors for human trypanosomiasis, commonly known as Chagas disease. Because of this, TrV is proposed as a biological control against this vector. The crystal structure of TrV was solved recently, but an omitted map of the structure, in the region of the 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 be responsible for the interaction between the interior and the exterior of the virus capsid, across a putative pore. Using molecular dynamics simulations, we have observed that the pore formed in this axis remains without water molecules in the region surrounded by a ring of Valines which creates a supposed hydrophobic gate. Also, we have found certain conditions where the axis is completely full of water molecules, 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. Combining different results we could explain the characteristics of the omitted map.