Triatoma Virus (TrV) self-aggregation at low PH: a possible electrostatic explanation

AGUIRRE, J; NEUMANN, E; YEPES-OCHOA, I; MARTI G.A; COSTABEL, M.D; VIGUERA A.R; GUERIN, D.M.A.

Long Beach, California

Congreso; Joint Meeting of the Biophysical Society 52nd Annual Meeting and 16th International Biophysics Congress; 2008

Abstract Triatoma virus (TrV) is a +ssRNA, non-enveloped virus of the insect virus family Dicistroviridae. TrV capsid has icosahedral T=1 pseudo T=3 symmetry, and is composed of three proteins named VP1, VP2 and VP3, which MW are 39, 37 and 33 kDa respectivelyIX. Here we report that TrV capsid is resistant at very acidic pH values, and at pH´s lower than 4.0 the virus particles aggregate without any noticeable structural change as analyzed under Transmission Electron Microscopy, Static and Dynamic Light cattering and Fluorescence Spectroscopy. In this study, we compute the capsid´s lectrostatic potential at different pH values, and we postulate that the virus aggregation at acidic pH is due to electrostatic effects