PROTEIN-STRUCTURE OF LYMPHOCYTIC CHORIOMENINGITIS VIRUS - EVIDENCE FOR A CELL-ASSOCIATED PRECURSOR OF THE VIRION GLYCOPEPTIDES
PROTEIN-STRUCTURE OF LYMPHOCYTIC CHORIOMENINGITIS VIRUS - EVIDENCE FOR A CELL-ASSOCIATED PRECURSOR OF THE VIRION GLYCOPEPTIDES
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DOI:
10.1016/0042-6822(79)90042-4
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发表时间:
1979-01-01
期刊:
影响因子:
3.7
通讯作者:
OLDSTONE, MBA
中科院分区:
文献类型:
--
作者:
BUCHMEIER, MJ;OLDSTONE, MBA
Immunoprecipitates of cells [baby hamster kidney BHK-21/13S] infected with lymphocytic choriomeningitis virus (LCMV) contain a 74,000-75,000 dalton glycopeptide (GP-C) which is not found in the virion. The relationship between GP-C and the virus structural glycopeptides GP-1 and GP-2 was studied by 2-dimensional peptide mapping and pulse-chase labeling. GP-C contained the peptides of both GP-1 and GP-2 indicating that it is a proteolytic cleavage precursor of the structural glycopeptides. Radiolabeled glucosamine or methionine incorporated into GP-C during a 1 h pulse period was demonstrated in GP-1 and GP-2 after a chase interval of 6 h. GP-1 and GP-2 are apparently the only major products of the cleavages of GP-C, as mixtures of the digests of GP-1 and GP-2 essentially reproduce the map of GP-C. Carbohydrate label incorporation into the viral glycopeptides showed that GP-C was relatively rich in mannose and glucosamine but poor in fucose and galactose. GP-1 contained glucosamine, fucose and galactose, while GP-2 contained glucosamine and fucose. By surface iodination and immunoprecipitation, only GP-1 was found on the surfaces of infected cells.