IFISUR   23398
INSTITUTO DE FISICA DEL SUR
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Possible pore in the 5-fold symmetry axis of Triatoma Virus Capsid. Comparison with membrane protein channels.
Autor/es:
JUAN FRANCISCO VISO; FERNANDO ZAMARREÑO; MARÍA J. AMUNDARAIN; DIEGO M.A. GUÉRIN; MARCELO D. COSTABEL
Lugar:
Salto
Reunión:
Workshop; VIII PosLatAm course: Membrane Lipids, Transporters, Channels?and all that crosstalk and Latin American Crosstalk in Biophysics and Physiology; 2015
Institución organizadora:
Sociedad de Biofísica Uruguaya y Sociedad Argentina de Biofísica
Resumen:
nViral capsids present different structures in nature, one of thesestructures presents full icosahedral symmetry which involves thepresence of several symmetry axis (two-fold, three-fold and five-fold).Particularly, we study the five-fold symmetry axis of the virus ofTriatoma Virus (TrV)[1] (Figure 1). We postulate that this axis could playthe role of a possible channel that regulates the interaction of the viruswith its environment. In our research we study the behaviour of this axisthrough molecular dynamics and saw that this pore presents various ofthe characteristics of membrane channels.One such characteristics is the way that channels regulates thepassage of molecules. This is achieved through hydrophobicaminoacids that control the flow. This mechanism is call HydrophobicGating and its present in various membrane channels like theProkaryotic mechanosensitive channels, the tetreameric cationchannels, pentameric ligand-gated ion channels among others.In our work, we found that TrV may present a pore in its five-foldsymmetry channel that is regulated by a ring of hydrophobic aminoacidsthat regulates between the open and close state of the channel byhydrating or dehydrating it