title: Study of the gag-coded polyproteins of type D retroviruses. Block of glycosylation inhibits the processing of major structural protein.
abstract: The study of the gag-coded glycosylated polyprotein (gPr78gag) from type D retrovirus-producing cells is reported. It is shown that glycosylation inhibitors tunicamycin and 2-deoxy-D-glucose are blocking the synthesis of gPr78gag. This demonstrates that gPr78gag is a N-glycan. The protein part of gPr78gag is supposedly identified (MW = 65 k). The inhibitors used partially stopped the processing of gag-coded polyprotein Pr78gag into core protein p27 as shown in pulse-chase experiments.
authors.affiliation: All-Union Cancer Research Center, Moscow, U.S.S.R.
authors.forename: P O
authors.initials: PO
authors.lastname: Ilyinskii
authors.forename: V A
authors.initials: VA
authors.lastname: Morozov
authors.forename: K V
authors.initials: KV
authors.lastname: Ilyin
mesh_terms: D003847:Deoxyglucose / Q000494:pharmacology; D015683:Gene Products, gag / Q000096:biosynthesis* / Q000187:drug effects / Q000378:metabolism; D006031:Glycosylation; D011134:Polysaccharides / Q000378:metabolism; D012190:Retroviridae / Q000187:drug effects / Q000378:metabolism*; D014415:Tunicamycin / Q000494:pharmacology
chemical_list: D015683:Gene Products, gag; D011134:Polysaccharides; D014415:Tunicamycin; D003847:Deoxyglucose