Electrostatic study of Triatoma virus aggregation mechanism.

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

Salta

Congreso; XXXIX Annual Meeting of The Argentinean Biophysical Society 2010, Workshop CeBEM & 3rd Latin American Protein Society Meeting.; 2010

SAB, LAPS y otras.

Triatoma virus (TrV) is a member of the insect virus family Dicistroviridae. TrV virions consist of a non-enveloped capsid that encloses the viral genome, a single molecule of linear positive sense single-stranded RNA. The capsid encloses 60 repeats of four structural proteins VP1, VP2, VP3 and a minor one VP0 of 39 kDa, 37 kDa, 33 kDa and 45 kDa, respectively forming a T=1 (pseudo-triangulation p=3) icosahedron of about 30 nm diameter. Because TrV is a viral pathogen of Triatoma infestans it has been proposed as a biological control for this blood-sucking reduviid bug, one of the most important vector of American human trypanosomiasis (Chagas disease). Electrostatic modeling is a computational tool in biophysical studies and has been largely used to extract relevant and meaningful information about the stability, dynamics, and interactions of protein–protein systems. In this work, we calculate the electrostatic energy for the interaction between TrV capsids at different pHs values and in this way, we propose for the viral particles an aggregation mechanism based in an electrostatic effect.