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PMID: 6312106 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Synthesis and processing of glycoprotein D of herpes simplex virus types 1 and 2 in an in vitro system.

Journal of virology ·Vol. 48 ·No. 2 ·1983-11-00 ·Pages 521-33

Matthews JT, Cohen GH, Eisenberg RJ

Abstract

We carried out studies of in vitro translation and processing of glycoprotein D (gD) of herpes simplex virus types 1 and 2 by using mRNA from cells infected for 6 h and a reticulocyte lysate translation system. Polypeptides of 49,000 daltons were immunoprecipitated with anti-gD-1 sera. Each in vitro-synthesized molecule had the same methionine tryptic peptide profile as the respective in vivo precursors, pgD-1 and pgD-2. In addition, the polypeptides synthesized in vitro were larger than the corresponding molecules synthesized in the presence of tunicamycin. This suggested that each of the gD polypeptides synthesized in vitro contained a transient N-terminal signal sequence. When the translation mixture was supplemented with pancreatic microsomes, each of the gD polypeptides was converted cotranslationally to a larger-molecular-weight form. Processing involved addition of three N-asparagine-linked oligosaccharides and removal of the signal peptide. When trypsin was added after in vitro processing, a polypeptide which was 3,000 daltons smaller than the in vitro-modified form of gD was immunoprecipitated. Experiments with endo-beta-N-acetylglucosaminidase H showed that this polypeptide still contained the three N-asparagine-linked oligosaccharides. Two monoclonal antibodies, 57S (group V) and 17O (group VII), were used to further orient gD in microsomes. The group V determinant was located in the trypsin-sensitive 3,000-dalton fragment, and the group VII determinant was located in the portion of gD which was protected from trypsin. We concluded that gD is oriented with the three glycosylation sites inside the vesicles and that 3,000 daltons containing the group V determinant are located outside. Immunofluorescence studies indicated that the group V determinant of gD is inside the plasma membrane of herpes simplex virus-infected cells and that the group VII determinant is outside. This cellular orientation is consistent with predictions based on the in vitro experiments.

MeSH Terms
Acetylglucosaminidase/pharmacology Cell Line Cell Membrane/analysis Cell-Free System Humans Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase Microsomes/analysis Oligosaccharides/analysis Peptides/analysis Protein Processing, Post-Translational Simplexvirus/metabolism Viral Envelope Proteins/analysis,biosynthesis,metabolism
Chemicals
Oligosaccharides Peptides Viral Envelope Proteins Acetylglucosaminidase Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Matthews J T
Cohen G H
Eisenberg R J
References (39)
39 references, click to expand
  1. Isolation of a herpes simplex virus-specific antigenic fraction which stimulates the production of neutralizing antibody.
    J Virol. 1972 Nov;10(5):1021-30 PMID: 4344251
  2. Inhibition of herpes simplex virus type 2 replication by thymidine.
    J Virol. 1974 Jul;14(1):20-5 PMID: 4365718
  3. A film detection method for tritium-labelled proteins and nucleic acids in polyacrylamide gels.
    Eur J Biochem. 1974 Jul 1;46(1):83-8 PMID: 4850204
  4. Translation of reovirus mRNA, poliovirus RNA and bacteriophage Qbeta RNA in cell-free extracts of mammalian cells.
    Methods Enzymol. 1974;30:709-23 PMID: 4369395
  5. Detection of a virus-specific antigen on the surface of herpes simplex virus-transformed cells.
    J Virol. 1975 Mar;15(3):668-70 PMID: 163379
  6. Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma.
    J Cell Biol. 1975 Dec;67(3):835-51 PMID: 811671
  7. Membrane proteins specified by herpes simplex viruses. I. Identification of four glycoprotein precursors and their products in type 1-infected cells.
    J Virol. 1976 Mar;17(3):991-1008 PMID: 176453
  8. An efficient mRNA-dependent translation system from reticulocyte lysates.
    Eur J Biochem. 1976 AUG 1;67(1):247-56 PMID: 823012
  9. Glycoproteins specified by herpes simplex virus type 1: their synthesis, processing and antigenic relatedness to HSV -2 glycoproteins.
    IARC Sci Publ. 1975;(11 Pt 1):49-61 PMID: 65316
  10. Synthesis and glycosylation in vitro of glycoprotein of vesicular stomatitis virus.
    Proc Natl Acad Sci U S A. 1977 Apr;74(4):1516-20 PMID: 193104
  11. The cell-free synthesis of herpesvirus-induced polypeptides.
    Virology. 1977 May 1;78(1):349-53 PMID: 193273
  12. Synchronised transmembrane insertion and glycosylation of a nascent membrane protein.
    Nature. 1977 Oct 27;269(5631):775-80 PMID: 200844
  13. Efficient cleavage and segregation of nascent presecretory proteins in a reticulocyte lysate supplemented with microsomal membranes.
    J Biol Chem. 1978 Jun 10;253(11):3753-6 PMID: 649601
  14. Type-common CP-1 antigen of herpes simplex virus is associated with a 59,000-molecular-weight envelope glycoprotein.
    J Virol. 1978 Jul;27(1):172-81 PMID: 80458
  15. Membrane assembly: synthesis and intracellular processing of the vesicular stomatitis viral glycoprotein.
    J Supramol Struct. 1977;7(3-4):353-70 PMID: 211348
  16. Synthesis and assembly of membrane glycoproteins: presence of leader peptide in nonglycosylated precursor of membrane glycoprotein of vesicular stomatitis virus.
    Proc Natl Acad Sci U S A. 1979 Feb;76(2):570-4 PMID: 218209
  17. The structural proteins and glycoproteins of herpesviruses: a review.
    IARC Sci Publ. 1978;(24 Pt 1):157-67 PMID: 376432
  18. Cell-free synthesis and membrane insertion of mouse H-2Dd histocompatibility antigen and beta 2-microglobulin.
    Cell. 1979 Aug;17(4):759-69 PMID: 90552
  19. Structural analysis of precursor and product forms of type-common envelope glycoprotein D (CP-1 antigen) of herpes simplex virus type 1.
    J Virol. 1979 Sep;31(3):608-20 PMID: 229243
  20. Effect of tunicamycin on herpes simplex virus glycoproteins and infectious virus production.
    J Virol. 1980 Apr;34(1):142-53 PMID: 6246250
  21. Cotranslational sequestration of egg white proteins and placental lactogen inside membrane vesicles.
    Ann N Y Acad Sci. 1980;343:192-209 PMID: 6930851
  22. Synthesis and processing of glycoproteins gD and gC of herpes simplex virus type 1.
    J Virol. 1980 Nov;36(2):429-39 PMID: 6253668
  23. Vesicular stomatitis virus glycoprotein is anchored in the viral membrane by a hydrophobic domain near the COOH terminus.
    Proc Natl Acad Sci U S A. 1980 Jul;77(7):3884-8 PMID: 6253998
  24. Comparative structural analysis of glycoprotein gD of herpes simplex virus types 1 and 2.
    J Virol. 1980 Aug;35(2):428-35 PMID: 6255183
  25. Mechanism of compartmentation of secretory proteins: transport of exocrine pancreatic proteins across the microsomal membrane.
    J Cell Biol. 1980 Dec;87(3 Pt 1):611-28 PMID: 7462318
  26. Transfer of proteins across membranes.
    Annu Rev Biochem. 1981;50:317-48 PMID: 7023361
  27. Biosynthesis of the erythrocyte anion transport protein.
    J Biol Chem. 1981 Nov 10;256(21):11337-44 PMID: 6793594
  28. Serological analysis of herpes simplex virus types 1 and 2 with monoclonal antibodies.
    Infect Immun. 1982 Jan;35(1):363-7 PMID: 6172383
  29. Mechanisms for the incorporation of proteins in membranes and organelles.
    J Cell Biol. 1982 Jan;92(1):1-22 PMID: 7035466
  30. Monoclonal antibodies to herpes simplex virus type 1 proteins, including the immediate-early protein ICP 4.
    Infect Immun. 1981 Dec;34(3):684-92 PMID: 6277788
  31. Effect of monoclonal antibodies on limited proteolysis of native glycoprotein gD of herpes simplex virus type 1.
    J Virol. 1982 Feb;41(2):478-88 PMID: 6176725
  32. Purification of glycoprotein gD of herpes simplex virus types 1 and 2 by use of monoclonal antibody.
    J Virol. 1982 Mar;41(3):1099-1104 PMID: 6284965
  33. Location of the structural genes for glycoproteins gD and gE and for other polypeptides in the S component of herpes simplex virus type 1 DNA.
    J Virol. 1982 Jul;43(1):41-9 PMID: 6287015
  34. Herpes simplex virus type-1 glycoprotein D gene: nucleotide sequence and expression in Escherichia coli.
    Science. 1982 Oct 22;218(4570):381-4 PMID: 6289440
  35. Cell surface expression of the influenza virus hemagglutinin requires the hydrophobic carboxy-terminal sequences.
    Cell. 1982 Sep;30(2):649-56 PMID: 6814764
  36. Identification of polypeptide precursors to HSV-1 glycoproteins by cell-free translation.
    J Gen Virol. 1982 Jan;58 Pt 1:217-22 PMID: 6292345
  37. Processing of herpes simplex virus type 1 glycoproteins: two-dimensional gel analysis using monoclonal antibodies.
    J Gen Virol. 1983 Apr;64 (Pt 4):873-86 PMID: 6300307
  38. Detailed analysis of the portion of the herpes simplex virus type 1 genome encoding glycoprotein C.
    J Virol. 1983 Feb;45(2):634-47 PMID: 6300426
  39. Glycopeptides of the type-common glycoprotein gD of herpes simplex virus types 1 and 2.
    J Virol. 1983 Jun;46(3):679-89 PMID: 6304338
Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
Published
1983-11-00
Pages
521-33
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC255376
Subset
IM
Grants
NIAID NIH HHS · AI-18289 · United States
NIDCR NIH HHS · DE-02623 · United States
NINDS NIH HHS · NS-07180 · United States
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