Structure of the reovirus cell-attachment protein: a model for the domain organization of sigma 1

Abstract

This report describes a model for the structure of the reovirus cell-attachment protein sigma 1. S1 gene nucleotide sequences were determined for prototype strains of the three serotypes of mammalian reoviruses. Deduced amino acid sequences of the S1-encoded sigma 1 proteins were then compared in order to identify conserved features of these sequences. Discrete regions in the amino-terminal two-thirds of sigma 1 sequence share characteristics with the fibrous domains of other cellular and viral proteins. Most of the amino-terminal one-third of sigma 1 sequence is predicted to form an alpha-helical coiled coil like that of myosin. The middle one-third of sigma 1 sequence appears more heterogeneous; it is predicted to form a large region of beta-sheet that is followed by a region which contains two short alpha-helical coiled coils separated by a smaller region of beta-sheet. The two beta-sheet regions are each proposed to form a cross-beta sandwich like that suggested for the rod domain of the adenovirus fiber protein (N. M. Green, N. G. Wrigley, W. C. Russell, S. R. Martin, and A. D. McLachlan, EMBO J. 2:1357-1365, 1983). The remaining carboxy-terminal one-third of sigma 1 sequence is predicted to form a structurally complex globular domain. A model is suggested in which the discrete regions of sigma 1 sequence are ascribed to morphologic regions seen in computer-processed electron micrographic images of the protein (R. D. B. Fraser, D. B. Furlong, B. L. Trus, M. L. Nibert, B. N. Fields, and A. C. Steven, J. Virol. 64:2990-3000, 1990.