Surface electrostatic potential of Triatoma Vírus (TrV) capsid and low pH- induced aggregation

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

Montevideo, Uruguay

Congreso; 6th International Conference of Biological Physics; 2007

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 Scattering and Fluorescence Spectroscopy. In this study, we compute the capsid´s electrostatic potential at different pH values, and we postulate that the virus aggregation at acidic pH is due to electrostatic effects.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 Scattering and Fluorescence Spectroscopy. In this study, we compute the capsid´s electrostatic potential at different pH values, and we postulate that the virus aggregation at acidic pH is due to electrostatic effects.