TY - JOUR
T1 - A membrane glycoprotein that accumulates intracellularly
T2 - Cellular processing of the large glycoprotein of LaCrosse virus
AU - Madoff, David H.
AU - Lenard, John
N1 - Funding Information:
We thank Drs. D. K. Miller, J. 0. Lampen and J. E. Rothman for their helpful discussions. We are also indebted to Roger Vanderoef and Marge Kmetz for their excellent technical assistance. This work was supported by grants from the National Institutes of Health and the National Foundation-March of Dimes.
Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.
PY - 1982/4
Y1 - 1982/4
N2 - The intracellular transport and certain posttranslational modifications of the large glycoprotein (G1) of LaCrosse virus (LAC) in BHK cells have been studied. G1 from released LAC virus was characterized by complex oligosaccharides (endo H-resistant) and covalently attached fatty acid. Only a small fraction of total cellular G1 was present on the baby hamster kidney cell surface. Cell-surface G1 contained complex oligosaccharides, while total G1 in infected cells contained largely unprocessed (endo H-sensitive) oligosaccharides. In addition, cell G1 contained significantly less fatty acid than virionassociated G1. Pulse-chase experiments showed that the oligosaccharides of G1 were processed to the complex form much more slowly than the oligosaccharides of the vesicular stomatitis virus (VSV) glycoprotein (G). In addition, transit of LAC G1 to the cell surface and into extracellular virions was two to three fold slower than the transit of VSV G. Thus LAC G1 accumulates intracellularly and is only slowly processed by intracellular processing enzymes. Treatment with monensin caused accumulation in the cell of a form of G1 with partial sensitivity toward endo H, suggesting that monensin may act to inhibit the glycosylation process directly.
AB - The intracellular transport and certain posttranslational modifications of the large glycoprotein (G1) of LaCrosse virus (LAC) in BHK cells have been studied. G1 from released LAC virus was characterized by complex oligosaccharides (endo H-resistant) and covalently attached fatty acid. Only a small fraction of total cellular G1 was present on the baby hamster kidney cell surface. Cell-surface G1 contained complex oligosaccharides, while total G1 in infected cells contained largely unprocessed (endo H-sensitive) oligosaccharides. In addition, cell G1 contained significantly less fatty acid than virionassociated G1. Pulse-chase experiments showed that the oligosaccharides of G1 were processed to the complex form much more slowly than the oligosaccharides of the vesicular stomatitis virus (VSV) glycoprotein (G). In addition, transit of LAC G1 to the cell surface and into extracellular virions was two to three fold slower than the transit of VSV G. Thus LAC G1 accumulates intracellularly and is only slowly processed by intracellular processing enzymes. Treatment with monensin caused accumulation in the cell of a form of G1 with partial sensitivity toward endo H, suggesting that monensin may act to inhibit the glycosylation process directly.
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U2 - 10.1016/0092-8674(82)90061-7
DO - 10.1016/0092-8674(82)90061-7
M3 - Article
C2 - 6284375
AN - SCOPUS:0019973887
SN - 0092-8674
VL - 28
SP - 821
EP - 829
JO - Cell
JF - Cell
IS - 4
ER -