Post-translational glycosylation of coronavirus glycoprotein E1: inhibition by monensin.

Niemann, Heiner; Boschek, Bruce; Evans, D. E.; Rosing, Mechthild; Tamura, Teruko; Klenk, Hans‐Dieter

doi:10.1002/j.1460-2075.1982.tb01346.x

Cited by 131 publications

(92 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Measurement of N-acetylgalactosaminyl : polypeptide transferase activity in subcellular fractions of hen oviduct (23), rat intestinal mucosa (33), and developing rat brain (34) showed presence of this enzyme in a smooth membrane fraction. Another line of evidence indicating that O-glycosylation takes place in smooth membrane fractions comes from recent work on viral glycoprotein maturation (29,40,60). In mammary gland explants, cycloheximide treatment inhibited immediately N-glycosylation, presumably due to lack of nascent polypeptide acceptors, whereas O-glycosylation continued for 30 min, a time period necessary for the movement of possible acceptor polypeptides from the rough endoplasmic reticulum 402 THE JOURNAL OF CELL BIOLOGY " VOLUME 98,1984 to the Golgi apparatus (71).…”

Section: Discussionmentioning

confidence: 99%

Cytochemical localization of terminal N-acetyl-D-galactosamine residues in cellular compartments of intestinal goblet cells: implications for the topology of O-glycosylation.

Roth¹

1984

The Journal of Cell Biology

216

101

View full text Add to dashboard Cite

The O-linked oligosaccharides of mucin-type glycoproteins contain N-acetyl-Dgalactosamine (GaINAc) that is not found in N-linked glycoproteins . Because Helix pornatia lectin interacts with terminal GaINAc, we used this lectin, bound to particles of colloidal gold, to localize such sugar residues in subcellular compartments of intestinal goblet cells. When thin sections of low temperature Lowicryl K4M embedded duodenum or colon were incubated with Helix pomatia lectin-gold complexes, no labeling could be detected over the cisternal space of the nuclear envelope and the rough endoplasmic reticulum . A uniform labeling was observed over the first and several subsequent cis Golgi cisternae and over the last (duodenal goblet cells) or the two last (colonic goblet cells) trans Golgi cisternae as well as forming and mature mucin droplets. However, essentially no labeling was detected over several cisternae in the central (medial) region of the Golgi apparatus . The results strongly suggest that core Oglycosylation takes place in cis Golgi cisternae but not in the rough endoplasmic reticulum . The heterogenous labeling for GaINAc residues in the Golgi apparatus is taken as evidence that termination of certain O-oligosaccharide chains by GaINAc occurs in trans Golgi cisternae .Glycoproteins can be classified according to the nature of the linkage between the oligosaccharide chains and the polypeptide. The two main families are those having oligosaccharide chains linked N-glycosidically from N-acetyl-D-glucosamine to the amide nitrogen of asparagine and those possessing oligosaccharide chains O-glycosidically linked from N-acetyl-D-galactosamine (GaINAc)' to the hydroxyl groups of serine and/or threonine (22,28,35,36,72). The biosynthesis of Nlinked glycoproteins is currently considered to be a single pathway involving the assembly ofa lipid linked oligosaccharide (1, 41, 42), the en bloc transfer of the oligosaccharide from the lipid carrier to the nascent peptide chain (31, 32, 55), the processing of the oligosaccharide chains by glycosidases (12,18,24,27,38,(63)(64)(65)(66)) and the addition of terminal sugars by glycosyltransferases (5, 44, 57). The establishment of the carbohydrate to protein linkage in N-glycosylation seems to be a cotranslational process located in the rough endoplasmic reticulum and later steps of the assembly are thought to occur mainly in the Golgi apparatus (2,22,28). Much less information is available about the assembly of the THE JOURNAL OF CELL BIOLOGY " VOLUME 98 FEBRUARY 1984 399-406 0The Rockefeller University Press -0021-9525/84/02/0399/08 $1 .00 oligosaccharide chains of O-linked glycoproteins and its topology . The initial glycosylation reaction in the synthesis of O-linked glycoproteins involves the direct transfer ofGaINAc from uridine diphosphate (UDP)-GaINAc to the polypeptide by a UDP-GaINAc: polypeptide transferase and does not require oligosaccharide preassembly nor lipid intermediates (22,23,25,36,37,58,67). Opinions vary among investigators, however, regarding the su...

show abstract

Section: Discussionmentioning

confidence: 99%

Cytochemical localization of terminal N-acetyl-D-galactosamine residues in cellular compartments of intestinal goblet cells: implications for the topology of O-glycosylation.

Roth¹

1984

The Journal of Cell Biology

216

101

View full text Add to dashboard Cite

show abstract

“…Coronaviruses such as IBV bud from intracellular membranes and their small glycoproteins, designated p23 for IBV, appear only in intracellular membranes in virus-infected cells (16,40). The sequences of cDNAs encoding p23 predict a polypeptide of 225 amino acids which has a short extracytoplasmic domain containing two sites for addition of N-linked oligosaccharides followed by three hydrophobic domains which are believed to span the membrane three times.…”

Section: Transport Of G Protein With the Cytoplasmic Domain Of A Coromentioning

confidence: 99%

Cytoplasmic domains of cellular and viral integral membrane proteins substitute for the cytoplasmic domain of the vesicular stomatitis virus glycoprotein in transport to the plasma membrane.

Puddington¹,

Machamer²,

Rose³

1986

The Journal of Cell Biology

View full text Add to dashboard Cite

Abstract. Oligonucleotide-directed mutagenesis was used to construct chimeric cDNAs that encode the extracellular and transmembrane domains of the vesicular stomatitis virus glycoprotein (G) linked to the cytoplasmic domain of either the immunoglobulin u membrane heavy chain, the hemagglutinin glycoprotein of influenza virus, or the small glycoprotein (023) of infectious bronchitis virus. Biochemical analyses and immunofluorescence microscopy demonstrated that these hybrid genes were correctly expressed in eukaryotic cells and that the hybrid proteins were transported to the plasma membrane. The rate of transport to the Golgi complex of G protein with an immunoglobulin # membrane cytoplasmic domain was approximately sixfold slower than G protein with its normal cytoplasmic domain. However, this rate was virtually identical to the rate of transport of ~m heavy chain molecules measured in the B cell line WEHI 231. The rate of transport of G protein with a hemagglutinin cytoplasmic domain was threefold slower than wild type G protein and G protein with a p23 cytoplasmic domain, which were transported at similar rates. The combined results underscore the importance of the amino acid sequence in the cytoplasmic domain for efficient transport of G protein to the cell surface. Also, normal cytoplasmic domains from other transmembrane glycoproteins can substitute for the G protein cytoplasmic domain in transport of G protein to the plasma membrane. The method of constructing precise hybrid proteins described here will be useful in defining functions of specific domains of viral and cellular integral membrane proteins.

show abstract

“…The monovalent carboxylic ionophore monensin has probably found the widest application. It is assumed that by blocking the intracellular transport, presumably somewhere within the Golgi apparatus, this com-© IRL Press Limited, Oxford, England. pound interferes with the biosynthesis of cellular membrane and secretory proteins (Ledger et al, 1980;Vassalli, 1977, 1978) and of the glycoproteins of several viruses, such as vesicular stomatitis virus, alphaviruses and coronaviruses (Johnson and Schlesinger, 1980;Straus and Lodish, 1980;Kaariainen et al, 1980;Niemann et al, 1982). However, with influenza virus, monensin did not inhibit glycoprotein processing and virus assembly (Alonso and Compans, 1981).…”

Section: Introductionmentioning

confidence: 99%

Inhibition of proteolytic cleavage of the hemagglutinin of influenza virus by the calcium-specific ionophore A23187.

Klenk¹,

Garten²,

Rott³

1984

The EMBO Journal

Self Cite

View full text Add to dashboard Cite

At calcium-specific ionophore A23187 concentrations of -0.25 tM [which still allow assembly and release of fowl plague virus (FPV) particles] post-translational proteolytic cleavage of the viral hemagglutinin precursor HA into the fragments HA1 and HA2 is inhibited. The resulting virus particles with uncleaved hemagglutinin, that cannot be obtained under normal conditions, provide a suitable substrate for in vitro assays of the protease sensitivity of the FPV hemagglutinin. Proteolytic activation is accomplished with trypsin. Treatment with cathepsin B at low pH yields aberrant cleavage products suggesting that the cellular cleavage enzyme is not of lysosomal origin. A protease that cleaves the FPV hemagglutinin in the correct place can be detected in lysates of MDBK cells. This enzyme is calcium dependent and has a neutral pH optimum.

show abstract

Post-translational glycosylation of coronavirus glycoprotein E1: inhibition by monensin.

Cited by 131 publications

References 26 publications

Cytochemical localization of terminal N-acetyl-D-galactosamine residues in cellular compartments of intestinal goblet cells: implications for the topology of O-glycosylation.

Cytochemical localization of terminal N-acetyl-D-galactosamine residues in cellular compartments of intestinal goblet cells: implications for the topology of O-glycosylation.

Cytoplasmic domains of cellular and viral integral membrane proteins substitute for the cytoplasmic domain of the vesicular stomatitis virus glycoprotein in transport to the plasma membrane.

Inhibition of proteolytic cleavage of the hemagglutinin of influenza virus by the calcium-specific ionophore A23187.

Contact Info

Product

Resources

About