Sigma 1 protein of mammalian reoviruses extends from the surfaces of viral particles.
Electron microscopy revealed structures consisting of long fibers topped with knobs extending from the surfaces of virions of mammalian reoviruses. The morphology of these structures was reminiscent of the fiber protein of adenovirus. Fibers were also seen extending from the reovirus top component and intermediate subviral particles but not from cores, suggesting that the fibers consist of either the mu 1C or sigma 1 outer capsid protein. Amino acid sequence analysis predicts that the reovirus cell attachment protein sigma 1 contains an extended fiber domain (R. Bassel-Duby, A. Jayasuriya, D. Chatterjee, N. Sonenberg, J. V. Maizell, Jr., and B. N. Fields, Nature [London] 315:421-423, 1985). When sigma 1 protein was released from viral particles with mild heat and subsequently obtained in isolation, it was found to have a morphology identical to that of the fiber structures seen extending from the viral particles. The identification of an extended form of sigma 1 has important implications for its function in cell attachment. Other evidence suggests that sigma 1 protein may occur in virions in both an extended and an unextended state.
Furlong
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Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts.
Nibert
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Fields
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D000595:Amino Acid Sequence; D036022:Capsid Proteins; D004586:Electrophoresis; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D010447:Peptide Hydrolases; D011991:Receptors, Virus / Q000502:physiology; D012087:Reoviridae / Q000648:ultrastructure*; D014764:Viral Proteins / Q000502:physiology*; D014771:Virion / Q000648:ultrastructure
D036022:Capsid Proteins; D011991:Receptors, Virus; D014764:Viral Proteins; C031728:sigma 1 protein, reovirus; D010447:Peptide Hydrolases