The proteins of purified preparations of reovirus type 3 have been examined using polyacrylamide gel electrophoresis. Preparations of cell-associated virus grown with foetal calf serum show three major peaks, λ, µ, σ, and several minor peaks. Preparations of released virus grown without foetal calf serum show only the three major peaks, suggesting that the minor peaks are not virus proteins.

Analysis of preparations of released virus labelled with both [C]lysine and [H] leucine shows that each of three major peaks contains more than one polypeptide chain. The molecular weights of the polypeptides are: 140,000 to 150,000 for the λ group, 75,000 to 85,000 for µ and 36,000 to 44,000 for σ, as determined by migration in 5% sodium dodecyl sulphate-polyacrylamide gels. There are at least eight polypeptide chains distributed as two in peak λ, three in peak µ, and three in peak σ.

Top component particles isolated during purification of virus show the same three protein peaks as demonstrated in complete virus. Virus cores produced by trypsin or chymotrypsin treatment of the virus lack µ-group polypeptides and some σ polypeptides.

Radioactive glucosamine and fucose are not incorporated into any of the three groups of virus particle proteins during the growth cycle. The content of amino sugar or methylpentose in purified virus is less than 0.1% and that of neutral carbohydrates less than 1%. These results indicate that purified preparations of reovirus type 3 contain little if any carbohydrate. Such purified preparations agglutinate ox red blood cells.


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