Inhibitors of protein glycosylation and glycoprotein processing in viral systems

Datema, Roelf; Olofsson, Sigvard; Romero, Pedro

doi:10.1016/0163-7258(87)90066-0

Cited by 83 publications

(85 citation statements)

References 437 publications

(491 reference statements)

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“…The signals or amino acid sequences that identify O-glycosylation sites are not well-defined. However, in general the amino acid sequence of a protein and the capacity of a cell to glycosylate a protein determine which potential glycosylation sites are used and the structure of the polysaccharides at these sites (Datema et al, 1987). It is likely that accessibility of specific serine or threonine residues to the N-acetylgalactosaminyl transferase plays a major role in determining whether these residues become O-glycosylated.…”

Section: Discussionmentioning

confidence: 99%

Processing of human cytomegalovirus envelope glycoproteins in and egress of cytomegalovirus from human astrocytoma cells

Kari

Radeke²,

Gehrz³

1992

Journal of General Virology

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The synthesis of human cytomegalovirus (HCMV) envelope glycoproteins and the production of infectious HCMV in human astrocytoma and skin fibroblast (SF) cells were analysed. HCMV envelope glycoproteins synthesized in astrocytoma cells had lower Mrs than the same glycoproteins synthesized in SF cells regardless of the strain of HCMV used, showing that the differences observed were due to differences in processing by the host cell and not the strain of HCMV used. HCMV envelope glycoproteins synthesized in astrocytoma cells were found to contain less galactosamine. Moreover, when synthesized in SF cells some HCMV glycoproteins contained a protease-resistant fragment owing to the presence of a cluster of O-linked oligosaccharides on the polypeptide. This fragment was not present when these HCMV glycoproteins were synthesized in astrocytoma cells. These data suggested that HCMV glycoproteins synthesized in astrocytoma cells contain fewer O-linked oligosaccharides. In contrast, other post-translational events such as proteolytic cleavage of the HCMV gB glycoprotein and the formation of disulphide-linked complexes did occur. The virus produced in astrocytoma ceils was capable of infecting SF cells, suggesting that complete O-glycosylation is not needed to produce infectious HCMV. However, astrocytoma cells were slow to release virus into the culture medium, suggesting that a fully functional Golgi network is needed for efficient egress of HCMV from the host cell.

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Section: Discussionmentioning

confidence: 99%

Processing of human cytomegalovirus envelope glycoproteins in and egress of cytomegalovirus from human astrocytoma cells

Kari

Radeke²,

Gehrz³

1992

Journal of General Virology

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“…The glycoproteins of enveloped viruses, being exposed both on the virion and on the surface of infected cells, constitute important targets for humoral and cellular immune responses (for a review, see Datema et al, 1987). As far as is known the carbohydrate composition even of genetically large viruses such as herpes simplex virus (HSV) is specified entirely by the host cell genome (Campadelli-Fiume & Serafini-Cessi, 1985;Lundstr6m et al, 1987b).…”

Section: Introductionmentioning

confidence: 99%

Activity of herpes simplex virus type 1-specified glycoprotein C antigenic site II epitopes reversibly modulated by peripheral fucose or galactose units of glycoprotein oligosaccharides

Olofsson

Sjöblom

Jeansson

1990

Journal of General Virology

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We have previously shown that the herpes simplex virus type 1 (HSV-1)-specified glycoprotein C (gC-1) produced in epitheloid cells contains epitopes of peptide nature, which are dependent on galactose of oligosaccharides for their expression. In the present communication we report that these epitopes are expressed in a mouse neuroblastoma cell line (C1300) with low levels of galactosyl transferases. However, in place of galactose the glycoprotein from C1300 cells was found to contain oligosaccharides with additional fucose units. Fucosidase treatment, but not galactosidase treatment, abolished the antigenic activity of the carbohydrate-dependent epitopes. Altogether the resuits indicated that the carbohydrate-dependent epitopes of gC-1 from C1300 cells were stabilized by peripheral sugars of N-linked oligosaccharides rather than O-linked ones and that fucose could substitute for terminal galactose in promoting the activity of the carbohydrate-dependent epitopes. This is the first demonstration of the involvement of fucose in the establishment of a carbohydrate-dependent epitope of peptide nature. The results also demonstrated that reversible carbohydrate-peptide interactions were responsible for the activity of the carbohydrate-dependent epitopes.

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“…The N-linked glycosylation pathway is well defined, consisting of over 13 enzymes that are involved in processing within the ER and the Golgi apparatus (6). Specific inhibitors of this pathway can be used to probe the importance of N-linked glycosylation.…”

mentioning

confidence: 99%

“…The ␣-glucosidases are the first enzymes involved in the glycan processing pathway and remove the terminal three glucose residues from the Glc 3 Man 9 GlcNAc 2 glycoform after it has been transferred from the dolichol diphosphate to the growing polypeptide backbone (reviewed in ref. 6). Sitedirected mutagenesis on the individual glycan sites of the three glycoproteins has allowed more detailed conclusions as to which glycosylation site is important in viral secretion.…”

mentioning

confidence: 99%

Hepatitis B virus (HBV) envelope glycoproteins vary drastically in their sensitivity to glycan processing: Evidence that alteration of a single N-linked glycosylation site can regulate HBV secretion

Mehta

Block

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

124

102

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Inhibitors of protein glycosylation and glycoprotein processing in viral systems

Cited by 83 publications

References 437 publications

Processing of human cytomegalovirus envelope glycoproteins in and egress of cytomegalovirus from human astrocytoma cells

Processing of human cytomegalovirus envelope glycoproteins in and egress of cytomegalovirus from human astrocytoma cells

Activity of herpes simplex virus type 1-specified glycoprotein C antigenic site II epitopes reversibly modulated by peripheral fucose or galactose units of glycoprotein oligosaccharides

Hepatitis B virus (HBV) envelope glycoproteins vary drastically in their sensitivity to glycan processing: Evidence that alteration of a single N-linked glycosylation site can regulate HBV secretion

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