Studies on benzhydrazone, a specific inhibitor of herpesvirus glycoprotein synthesis. Size distribution of glycopeptides and endo-β-N-acetylglucosaminidase-H treatment

Serafini‐Cessi, Franca; Campadelli-Fiume, Gabriella

doi:10.1007/bf01320248

Cited by 37 publications

(25 citation statements)

References 36 publications

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“…It has been shown that the modified inner nuclear membrane and associated enveloping nucleocapsids contain Nlinked oligosaccharides [4,12,24,30,39]. It also has been reported that such precursor viral glycoproteins have antigenic sites related to viral glycoprotein G (gG) and mannose [25,26].…”

Section: Discussionmentioning

confidence: 99%

Ultrastructural localization of glycoproteins in rabbit fibroblasts altered by Herpes simplex virus type 1 infection

López‐Iglesias

Puvion‐Dutilleul

1988

Biology of the Cell

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The periodic acid-thiocarbohydrazide (SO2)--OsO4 method was used to examine the distribution of glycoproteins in rabbit fibroblast cells infected with Herpes simplex virus type 1. In non-infected cells, a low level of staining was seen over the plasma membrane and the membranes of the Golgi apparatus. At 17 hr post-infection, the intensity of reaction was increased to include not only a relatively heavy staining of the plasma membrane, including the numerous microvilli characteristic of infected cells, and of the newly proliferated Golgi membranes, but also the envelopes of intracytoplasmic and extracellular virions. A very faint but only occasional staining also was associated with the virus-induced reduplications of the inner nuclear membrane and the envelopes of associated enveloping nucleocapsids. We suggest that such differences in the intensity of staining may be related either to the amount of glycoproteins or to the sequential maturation of the viral glycoproteins. We also observed that the structurally modified portions of the Golgi membranes at the position where intracytoplasmic naked nucleocapsids bud into the Golgi cisternae usually exhibit a more intense reaction for glycoproteins than do the adjacent portions of the Golgi membranes. This supports the evidence for an envelopment of nucleocapsids in the cytoplasm, but it does not indicate whether this event obligatorily follows or only occasionally takes the place of the envelopment of nucleocapsids at the inner nuclear membrane. In either event, the envelopes of all mature virions exhibit a prominent reaction to glycoproteins.

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Section: Discussionmentioning

confidence: 99%

Ultrastructural localization of glycoproteins in rabbit fibroblasts altered by Herpes simplex virus type 1 infection

López‐Iglesias

Puvion‐Dutilleul

1988

Biology of the Cell

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“…Cells infected with herpes simplex virus provide a useful system for investigating the processes discussed above. Previous studies have shown that glycoproteins specified by herpes simplex virus type 1 (HSVl) contain O-linked oligosaccharides (Oloffson et al, 1981) as well as N-linked oligosaccharides (Pizer et al, 1980;Serafini-Cessi and Campadelli-Fiume, 1981;Person et al, 1982;Wenske et al, 1982). We have confirmed these findings, further characterized the O-linked oligosaccharides and shown that 3H-palmitate is incorporated into one of the HSVl glycoproteins.…”

Section: Introductionmentioning

confidence: 99%

O-linked oligosaccharides are acquired by herpes simplex virus glycoproteins in the Golgi apparatus

Johnson¹,

Spear²

1983

Cell

283

189

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The O-linked oligosaccharides on mature forms of herpes simplex virus type 1 (HSV1) glycoproteins were characterized, and were found to account largely for the lower electrophoretic mobilities of these forms relative to the mobilities of immature forms. Other posttranslational modifications of HSV1 glycoproteins (designated gB, gC, gD and gE) were related temporally to the discrete shifts in electrophoretic mobilities that signal acquisition of the O-linked oligosaccharides. Fatty acid acylation (principally of gE) could be detected just prior to the shifts, whereas conversion of high-mannose-type N-linked oligosaccharides to the complex type occurred coincident with the shifts. The addition of O-linked oligosaccharides did not occur in cells treated with the ionophore monensin or in a ricin-resistant cell line defective in the processing of N-linked oligosaccharides. We conclude that extension of O-linked oligosaccharide chains on HSV1 glycoproteins, and probably also attachment of the first O-linked sugars, occurs as a late posttranslational modification in the Golgi apparatus.

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“…For gA/B, gC and gD, this suggestion is supported by the observation (Serafini-Cessi & Campadelli-Fiume, 1981 ;Person et al, 1982;Wenske et al, 1982) that the partially glycosylated precursors are sensitive to endoglycosidase H, an enzyme that cleaves high mannose asparagine-N-linked oligosaccharides from the polypeptide backbone. Glycoprotein C was shown by affinity chromatography on soybean and Helix pomatia lectins to possess, in addition, a terminal N-acetylgalactosamine sugar suggestive of O-glycosidically attached sugars (Olafsson et al, 1981).…”

Section: Introductionmentioning

confidence: 82%

Processing of Glycoproteins Induced by Herpes Simplex Virus Type 1: Sulphation and Nature of the Oligosaccharide Linkages

Hope

Marsden

1983

Journal of General Virology

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SUMMARYUsing the drug tunicamycin we have investigated the nature of the oligosaccharides on herpes simplex virus type 1 (HSV-1)-induced glycoproteins E and Y (gY is a newly identified glycoprotein which has the same apparent mol. wt. as gC but a more basic isoelectric point). Synthesis of both glycoproteins was inhibited by the drug, suggesting they contain N-linked oligosaccharides. Our finding, combined with the previous results of other workers, suggests that all the major HSV-induced glycoproteins have this type of carbohydrate modification. All of the major HSV-1-induced glycoproteins are modified by addition of inorganic sulphate. This modification occurs late in their maturation. Most inorganic sulphate appears to be attached to N-linked oligosaccharides but some is attached to other parts of glycoprotein E. Using HSV-1/HSV-2 intertypic recombinants, the mapping limits of that part of the glycoprotein E gene coding for differences in mobility between the two serotypes have been further narrowed and are located between coordinates 0.886 and 0-935.

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Studies on benzhydrazone, a specific inhibitor of herpesvirus glycoprotein synthesis. Size distribution of glycopeptides and endo-β-N-acetylglucosaminidase-H treatment

Cited by 37 publications

References 36 publications

Ultrastructural localization of glycoproteins in rabbit fibroblasts altered by Herpes simplex virus type 1 infection

Ultrastructural localization of glycoproteins in rabbit fibroblasts altered by Herpes simplex virus type 1 infection

O-linked oligosaccharides are acquired by herpes simplex virus glycoproteins in the Golgi apparatus

Processing of Glycoproteins Induced by Herpes Simplex Virus Type 1: Sulphation and Nature of the Oligosaccharide Linkages

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