Preliminary results in the hidratation of the hydrophobic region of the 5-fold symmetry axis of TrV.

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

Villa Carlos Paz

Congreso; XLII Reunión Anual de la Sociedad Argentina de Biofísica; 2013

Sociedad Argentina de Biofísica

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 kind of insects. In this work we study the capsid of TrV, which is an icosahedral structure formed by multiple copies of the proteins (Vp1, Vp2 and Vp3). In particular we are interested in the 5-fold symmetry axis because of the channel formed along this axis may be responsible of the interaction of the interior of the virus with the exterior. Previously we have observed that the pore formed in this axis remains closed in the position of a ring of aminoacids formed by Valines which created an hydrophobic gate. Using molecular dynamics we have found certain conditions where the axis is completely full of water molecules, even in the hydrophobic region. The complete hydratation of the channel may lead to the opening of the channel and the interaction between the interior and the exterior of the capsid.