Analysis of the five-fold symmetry axis of icosahedral virus capsids

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

Caxambú

Otro; Reunión Anual de la Federación de Sociedades de Biología Experimental.; 2014

Federación de Sociedades de Biología Experimental.

Viral capsids play a crucial role in the process of viral infection, nevertheless, very little is known ofthis process. To understand this mechanism, better comprehension of the structural properties isneeded. In this work we study the structure of different viral capsids and compare theirtridimensional configuration as well as their aminoacids composition and properties.Viruses from the picornavirales genus were selected for this study. The selected virus wereTriatoma Virus (TrV, 3NAP)[1], Cricket Paralysis Virus (CrPV, 1B35)[2], Human Rhinovirus (HRV1,1R1A)[3] and Bean-Pod Mottle Virus (BPMV, 1BMV)[4]. The first three are animals virus while the lastone is a plant virus. Others picornavirales viruses structures were studied as well but only payingattention to their crystallographic structure.In particular we focus our study in Triatoma Virus and compare it with the other viruses. The reasonfor studing TrV is because it infects several species of triatomine insects, which are the vectors forhuman trypanosiomiasis, commonly known as Chagas Disease. Because of this TrV is proposed asa biological control against this kind of insects. For this reason it is important to better understandits structure.