Sigma 1 protein of mammalian reoviruses extends from the surfaces of viral particles

Journal Article · Fri Jan 01 00:00:00 EST 1988 · J. Virol.; (United States)

OSTI ID:5442445

Furlong, D B; Nibert, M L; Fields, B N

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 sigma1 outer capsid protein. Amino acid sequence analysis predicts that the reovirus cell attachment protein sigma1 contains an extended fiber domain. When sigma1 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 sigma1 has important implications for its function in cell attachment. Other evidence suggest that sigma1 protein may occur in virions in both an extended and an unextended state.

• Research Organization: Harvard Medical School, Boston, MA
• OSTI ID: 5442445
• Journal Information: J. Virol.; (United States), Vol. 62:1
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
PROTEINS
ELECTRON MICROSCOPY
MOLECULAR STRUCTURE
PURIFICATION
VIRUSES
ELECTROPHORESIS
MICE
SCANNING ELECTRON MICROSCOPY
SULFUR 35
TRANSMISSION ELECTRON MICROSCOPY
ANIMALS
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
DAYS LIVING RADIOISOTOPES
EVEN-ODD NUCLEI
ISOTOPES
LIGHT NUCLEI
MAMMALS
MICROORGANISMS
MICROSCOPY
NUCLEI
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PARASITES
RADIOISOTOPES
RODENTS
SULFUR ISOTOPES
VERTEBRATES
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