Synthesis of proteins in cells infected with herpesvirus

Erickson, John S.; Kaplan, Albert S.

doi:10.1016/s0042-6822(73)81011-6

Cited by 22 publications

(11 citation statements)

References 15 publications

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“…The results presented show that HSV glycoproteins, like the proteins of many viruses (Erickson & Kaplan, 1973;Compans & Pinter, 1975;Pinter & Compans, 1975;Pennington & McCrae, 1977), are sulphated. Glycoprotein E which has affinity for the Fc region of immunoglobin (Baucke & Spear, 1979) is the major sulphated glycoprotein in BHK cells infected with either 17 syn + (HSV-1) or HG52 (HSV-2).…”

Section: Discussionmentioning

confidence: 78%

“…Glycoproteins are excreted from cells infected with at least three different herpesviruses: HSV (Kaplan et al, 1975;Chen et al, 1978;Norrild & Vertergaard, 1979;Randall et al, 1980), pseudorabies (Erickson & Kaplan, 1973;Pennington & McCrae, 1977) and herpesvirus saimiri (Randall & Honess, 1980). We show here that a subset of HSV-induced sulphated glycoproteins are excreted.…”

Section: G Hope and Othersmentioning

confidence: 99%

“…Inorganic sulphate is incorporated into glycoproteins of several virus groups including paramyxoviruses (simian virus 5 and Sendai), rhabdoviruses (vesicular stomatitis virus), togaviruses (Sindbis), oncornaviruses (Rauscher leukaemia virus) (Pinter & Compans, 1975), orthomyxoviruses (influenza virus) (Compans & Pinter, 1975) and one member of the herpesvirus group (pseudorabies) (Erickson & Kaplan, 1973;Pennington & McCrae, 1977). Therefore, we decided to investigate whether sulphation plays a role in the processing of any HSV glycoproteins.…”

Section: Introductionmentioning

confidence: 99%

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Sulphated Glycoproteins Induced by Herpes Simplex Virus

Hope

Palfreyman

Suh³

et al. 1982

Journal of General Virology

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SUMMARYBHK cells infected with strain 17 syn + (HSV-1) or HG52 (HSC-2)incorporated inorganic sulphate into polypeptides which co-migrated on SDS-polyacrylamide gels with virus-induced glycoproteins. The major sulphated glycoprotein was glycoprotein E. In addition, less-intense sulphated bands co-migrated with glycoprotein D and HSV-1 glycoprotein A/B/C. Sulphate label co-migrating with HSV-2 glycoprotein A/B/C was occasionally observed. We have investigated which sulphated polypeptides are excreted from infected cells. Major ones of apparent mol. wt. 32000, 34000 and 35000 were excreted from cells infected with 17 syn +. In addition, polypeptides which migrated in the vicinity of glycoprotein D were often excreted from cells infected with either 17 syn + or HG52. The 32K, 34K and 35K polypeptides were antigenically related to glycoprotein D and over 95 % of the total amount synthesized was excreted. Analysis of intracellular sulphated polypeptides using intertypic recombinants mapped glycoprotein E to between 0-832 and 0-950 units of the HSV genome.

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Section: Discussionmentioning

confidence: 78%

Section: G Hope and Othersmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Sulphated Glycoproteins Induced by Herpes Simplex Virus

Hope

Palfreyman

Suh³

et al. 1982

Journal of General Virology

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“…may also prevent it from entering. Synthesis of mucopolysaccharide is rapidly inhibited in cells infected with pseudorabies virus (Erickson & Kaplan, 1973) or HSV ( Fig. 2 and Hope et al, 1982).…”

Section: Discussionmentioning

confidence: 97%

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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“…Neither the secreted 34-kDa HSV-2 gG component nor PRV gG was found associated with purified virions. A hitherto unique feature of PRV gG is the addition of sulfate groups (5,12,31), which was hypothesized to occur at tyrosine residues of the protein backbone (5). In this report, we identify transcripts encompassing the BHV-1 U S ORF4 and identify and characterize BHV-1 U S ORF4 gene products.…”

mentioning

confidence: 93%

Bovine herpesvirus 1 U(s) open reading frame 4 encodes a glycoproteoglycan

Keil¹,

Engelhardt²,

Karger³

et al. 1996

J Virol

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Sequence analysis of the short unique (U S ) segment of the bovine herpesvirus 1 (BHV-1) genome predicted that the U S open reading frame (ORF) 4 encodes a protein with homology to glycoprotein G (gG) of other alphaherpesviruses (P. Leung-Tack, J.-C. Audonnet, and M. Riviere, Virology 199:409-421, 1994). RNA analysis showed that the U S ORF4 is contained within two transcripts of 3.5 and 1.8 kb. The 3.5 kb RNA represents a structurally bicistronic RNA which encompasses the U S ORF3 and U S ORF4, whereas the 1.8-kb RNA constitutes the monocistronic U S ORF4 mRNA. To identify the predicted BHV-1 gG, recombinant vaccinia virus expressing the U S ORF4 was used to raise specific antibodies in rabbits. The antiserum recognized a 65-kDa polypeptide and a very diffusely migrating species of proteins with an apparent molecular mass of between 90 and greater than 240 kDa in supernatants of BHV-1-infected cells which was also precipitated together with 61and 70-kDa polypeptides from cell-associated proteins. The specificity of the reaction was demonstrated by the absence of these proteins from the supernatant of cells infected with the U S ORF4 deletion mutant BHV-1/ gp1-8. Treatment of the immunoprecipitated proteins with glycosidases and chondroitinase AC showed that the 65-kDa protein constitutes gG, which contains both N-and O-linked carbohydrates, and that the highmolecular-mass proteins contain glycosaminoglycans linked to a 65-kDa glycoprotein that is antigenically related to gG. These molecules were therefore named glycoproteoglycan G (gpgG). Pulse chase experiments indicated that gG and gpgG were processed from a common precursor molecule with an apparent molecular mass of 61 kDa via a 70-kDa intermediate. Both gG and gpgG could not be found associated with purified virions. In summary, our results identify the BHV-1 gG protein and demonstrate the presence of a form of posttranslational modification, glycosamino-glycosylation, that has not yet been described for a herpesvirusencoded protein.

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Synthesis of proteins in cells infected with herpesvirus

Cited by 22 publications

References 15 publications

Sulphated Glycoproteins Induced by Herpes Simplex Virus

Sulphated Glycoproteins Induced by Herpes Simplex Virus

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

Bovine herpesvirus 1 U(s) open reading frame 4 encodes a glycoproteoglycan

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