The synthesis of complex-type oligosaccharides. II. Characterization of the processing intermediates in the synthesis of the complex oligosaccharide units of the vesicular stomatitis virus G protein.
TL;DR: To elucidate the sequence of processing, pulse-chase experiments were performed with virus-infected Chinese hamster ovary cells using labeled mannose, glucosamine, and galactose and demonstrated that processing is initiated by the rapid removal of 2 of the 3 glucose residues of the precursor oligosaccharide.
About: This article is published in Journal of Biological Chemistry.The article was published on 1978-11-10 and is currently open access. It has received 331 citations till now. The article focuses on the topics: Vesicular stomatitis virus & Oligosaccharide.
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University of California, San Diego1, Harvard University2, ETH Zurich3, Macquarie University4, Max Planck Society5, Albert Einstein College of Medicine6, Johns Hopkins University7, University of Georgia8, Osaka University9, Discovery Institute10, University of California, Santa Barbara11, Stanford University12, University of California, Davis13, Utrecht University14, University of Giessen15, University of Grenoble16, National Institutes of Health17, Scripps Research Institute18, Kyoto University19, Soka University of America20, Imperial College London21, National Institute of Advanced Industrial Science and Technology22, Washington University in St. Louis23
TL;DR: Author(s): Varki, Ajit; Cummings, Richard D; Aebi, Markus; Packer, Nicole H; Seeberger, Peter H; Esko, Jeffrey D; Stanley, Pamela; Hart, Gerald; Darvill, Alan; Kinoshita, Taroh; Prestegard, James J; Schnaar, Ronald L; Freeze, Hudson H; Marth, Jamey D; Bertozzi, Carolyn R.
Abstract: Author(s): Varki, Ajit; Cummings, Richard D; Aebi, Markus; Packer, Nicole H; Seeberger, Peter H; Esko, Jeffrey D; Stanley, Pamela; Hart, Gerald; Darvill, Alan; Kinoshita, Taroh; Prestegard, James J; Schnaar, Ronald L; Freeze, Hudson H; Marth, Jamey D; Bertozzi, Carolyn R; Etzler, Marilynn E; Frank, Martin; Vliegenthart, Johannes Fg; Lutteke, Thomas; Perez, Serge; Bolton, Evan; Rudd, Pauline; Paulson, James; Kanehisa, Minoru; Toukach, Philip; Aoki-Kinoshita, Kiyoko F; Dell, Anne; Narimatsu, Hisashi; York, William; Taniguchi, Naoyuki; Kornfeld, Stuart
735 citations
Cites background from "The synthesis of complex-type oligo..."
...In 1978, Kornfeld and colleagues put forward an elegant and simple system for representation of vertebrate glycans (Kornfeld et al. 1978), and it entered into popular use over the next two decades....
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TL;DR: Transport of the VSV-encoded glycoprotein between successive compartments of the Golgi has been reconstituted in a cell-free system and is measured, in a rapid and sensitive new assay, by the coupled incorporation of 3H-N-acetylglucosamine (GlcNAc).
650 citations
Cites background from "The synthesis of complex-type oligo..."
...In this Tabas and Kornfeld, 1978), missing the Golgi enzymeand two following papers (Braell et al., 1984; Balch et al., GlcNAc transferase I....
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TL;DR: This chapter elaborates the primary structure and metabolism of the N -linked glycans, and presents the hypothesis that the catabolism of N -acetyl-lactosainine glycans starts by the action of endo-2-acetamido- 2-deoxy-β- D -glucosidases in liberating oligosaccharides that are then degraded by exoglycosidases.
Abstract: Publisher Summary This chapter provides an overview of the primary structure of glycoprotein glycans. There exists a certain unity of structure among glycans. All are derived by the substitution of common, core oligosaccharides ( inv fractions) by variable oligosaccharide structures ( var fractions), which are the basis of their specificity. The var fractions present a limited number of the types of structure. In the case of N -glycosylproteins, in which the glycan-protein bond is asparaginyl-2-acetamido-2-deoxyglucose, the glycans are of three fundamental types: the oligomannosidic, the N -acetyllactosaminic, and the mixed, oligomannosidic- N -acetyl-lactosaminic. The determination of the structures of oligosaccharides from the urines of glycoproteinoses, diseases characterized by a deficit in lysosomal enzymes catabolizing the glycans of glycoprotein, allows reconstruction of the different stages of glycoprotein catabolism, and presentation of the hypothesis that the catabolism of N -acetyl-lactosainine glycans starts by the action of endo-2-acetamido-2-deoxy-β- D -glucosidases in liberating oligosaccharides that are then degraded by exoglycosidases. This chapter elaborates the primary structure and metabolism of the N -linked glycans. Development and improvement of procedures for the study of the primary structure of glycans is also discussed.
528 citations
TL;DR: Baby hamster kidney cells were infected with Semliki Forest virus and treated for 4 h with 10 microM monensin, and it is suggested that the Golgi stack can be divided into three functionally distinct compartments, each comprising one or two cisternae.
Abstract: Baby hamster kidney (BHK) cells were infected with Semliki Forest virus (SFV) and, 2 h later, were treated for 4 h with 10 microM monensin. Each of the four to six flattened cisternae in the Golgi stack became swollen and separated from the others. Intracellular transport of the viral membrane proteins was almost completely inhibited, but their synthesis continued and they accumulated in the swollen Golgi cisternae before the monensin block. In consequence, these cisternae bound large numbers of viral nucleocapsids and were easily distinguished from other swollen cisternae such as those after the block. These intracellular capsid-binding membranes (ICBMs) were not stained by cytochemical markers for endoplasmic reticulum (ER) (glucose-6-phosphatase) or trans Golgi cisternae (thiamine pyrophosphatase, acid phosphatase) but were labeled by Ricinus communis agglutinin I (RCA) in thin, frozen sections. Since this lectin labels only Golgi cisternae in the middle and on the trans side of the stack (Griffiths, G., R. Brands, B. Burke, D. Louvard, and G. Warren, 1982, J. Cell Biol., 95:781-792), we conclude that ICBMs are derived from Golgi cisternae in the middle of the stack, which we term medial cisternae. The overall movement of viral membrane proteins appears to be from cis to trans Golgi cisternae (see reference above), so monensin would block movement from medial to the trans cisternae. It also blocked the trimming of the high-mannose oligosaccharides bound to the viral membrane proteins and their conversion to complex oligosaccharides. These functions presumably reside in trans Golgi cisternae. This is supported by data in the accompanying paper, in which we also show that fatty acids are covalently attached to the viral membrane proteins in the cis or medial cisternae. We suggest that the Golgi stack can be divided into three functionally distinct compartments, each comprising one or two cisternae. The viral membrane proteins, after leaving the ER, would all pass in sequence from the cis to the medial to the trans compartment.
407 citations
TL;DR: The synthesis of the complex-type oligosaccharide unit of the vesicular stomatitis virus G protein is initiated by the en bloc transfer of a high molecular weight oligosACcharide from a lipid carrier to the nascent polypeptide.
398 citations
References
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TL;DR: A surprisingly precise sequence by which the nascent chain of this membrane glycoprotein is glycosylated in two steps is revealed, which has important implications for the mechanisms of membrane assembly.
Abstract: Studies of the synthesis and incorporation of the vesicular stomatitis virus glycoprotein into membranes in a synchronised cell-free system demonstrate a tight coupling between polypeptide synthesis and membrane insertion, as a result of which the nascent chain crosses the membrane. The studies reveal a surprisingly precise sequence by which the nascent chain of this membrane glycoprotein is glycosylated in two steps. These findings have important implications for the mechanisms of membrane assembly.
506 citations
TL;DR: It is proposed that during glycosylation of asparagine residues, a common oligosaccharide is transferred from the lipid carrier to protein and is subsequently processed to yield the so-called "high mannose" and "complex" oligOSaccharides.
452 citations
403 citations
TL;DR: The synthesis of the complex-type oligosaccharide unit of the vesicular stomatitis virus G protein is initiated by the en bloc transfer of a high molecular weight oligosACcharide from a lipid carrier to the nascent polypeptide.
398 citations
TL;DR: Experiments performed with mouse LPCl cells which secrete IgG demonstrated a similar sequence of processing of the oligosaccharide units of this immunoglobulin, indicating that processing is probably a general phenomenon.
339 citations