PMC:7499584 / 2389-4428
Annnotations
{"target":"http://pubannotation.org/docs/sourcedb/PMC/sourceid/7499584","sourcedb":"PMC","sourceid":"7499584","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7499584","text":"Schwartz reported, in 1974, tunicamycin inhibition of glycosylation of influenza virus hemagglutinin (Schwartz et al. 1974) and in 1976 showed that tunicamycin, which inhibits the formation of N-acetylglucosamine-lipid intermediates in N-linked glycan synthesis (Lennarz 1975), suppressed glycoprotein synthesis in Semliki Forest, influenza and avian sarcoma virus (Schwarz et al. 1976). Kornfeld et al. (1977) examined the effect of tunicamycin (Leavitt et al. 1977a) on growth of Sindbis and VSV in BHK cells and found at 500 ng/ml, 99.9% inhibition of replication without detection of non-infectious particles (Leavitt et al. 1977b). Viral proteins were synthesized, but glycoproteins were under-glycosylated (Leavitt et al. 1977b) and temperature sensitive (Gibson et al. 1979). Their conclusion was that in enveloped viruses, glycosylation was essential for normal viral particle assembly. Morrison et al. (1978) found that tunicamycin had no effect on glycoprotein attachment to intracellular membranes or protein transport to the endoplasmic reticulum lumen, but instead prevented glycoprotein migration from the rough to smooth. Kornfeld et al. (1979) found that VSV non-glycosylated glycoprotein underwent intracellular aggregation upon tunicamycin treatment (Gibson et al. 1979), an indication of improper folding or exposure of hydrophobic peptide due to pauciglycosylation. Diggelman (1979) showed biosynthesis of an unglycosylated envelope glycoprotein of Rous sarcoma virus in the presence of tunicamycin. Pizer et al. (1980) showed that tunicamycin inhibited production of infectious herpes simplex virus-1 (HSV1). Blocking addition of carbohydrate to glycoprotein precursors with tunicamycin resulted in disappearance of proteins, postulated due to degradation of unglycosylated polypeptides. They concluded that the glycans either stabilize the envelope proteins or provide proper structure for processing of the proteins necessary for infectivity. Stallcup and Fields (1981) inhibited measles virus with tunicamycin (24).","tracks":[{"project":"2_test","denotations":[{"id":"32829416-4372604-45163144","span":{"begin":118,"end":122},"obj":"4372604"},{"id":"32829416-167438-45163145","span":{"begin":271,"end":275},"obj":"167438"},{"id":"32829416-218976-45163149","span":{"begin":776,"end":780},"obj":"218976"},{"id":"32829416-212608-45163150","span":{"begin":912,"end":916},"obj":"212608"},{"id":"32829416-218976-45163151","span":{"begin":1283,"end":1287},"obj":"218976"},{"id":"32829416-7467126-45163152","span":{"begin":1987,"end":1991},"obj":"7467126"},{"id":"T44068","span":{"begin":118,"end":122},"obj":"4372604"},{"id":"T5449","span":{"begin":271,"end":275},"obj":"167438"},{"id":"T65958","span":{"begin":776,"end":780},"obj":"218976"},{"id":"T40017","span":{"begin":912,"end":916},"obj":"212608"},{"id":"T65471","span":{"begin":1283,"end":1287},"obj":"218976"},{"id":"T72045","span":{"begin":1987,"end":1991},"obj":"7467126"}],"attributes":[{"subj":"32829416-4372604-45163144","pred":"source","obj":"2_test"},{"subj":"32829416-167438-45163145","pred":"source","obj":"2_test"},{"subj":"32829416-218976-45163149","pred":"source","obj":"2_test"},{"subj":"32829416-212608-45163150","pred":"source","obj":"2_test"},{"subj":"32829416-218976-45163151","pred":"source","obj":"2_test"},{"subj":"32829416-7467126-45163152","pred":"source","obj":"2_test"},{"subj":"T44068","pred":"source","obj":"2_test"},{"subj":"T5449","pred":"source","obj":"2_test"},{"subj":"T65958","pred":"source","obj":"2_test"},{"subj":"T40017","pred":"source","obj":"2_test"},{"subj":"T65471","pred":"source","obj":"2_test"},{"subj":"T72045","pred":"source","obj":"2_test"}]}],"config":{"attribute types":[{"pred":"source","value type":"selection","values":[{"id":"2_test","color":"#ecb493","default":true}]}]}}