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. 2004 Jun 9;131(1):230–241. doi: 10.1016/0042-6822(83)90548-2

A study of the glycoproteins of Autographa californica nuclear polyhedrosis virus (AcNPV)

Brad Stiles 1,1, HA Wood 1
PMCID: PMC7131021  PMID: 18639173

Abstract

Pulse labeling with tritiated mannose was used to follow the time course of Autographa californica nuclear polyhedrosis virus (AcNPV) glycoprotein synthesis in Spodoptera frugiperda IPLB-21 cells. Nine viral-induced intracellular glycoproteins were first detected from as early as 2 hr postinoculation (67K, early phase) to as late as 14 hr (36K and 19K glycoproteins, intermediate phase). Glycosylation of these proteins was observed to continue to the end of the experiment (28 hr postinoculation). Seven of these intracellular glycoproteins could also be detected in infected Trichoplusia ni TN-368 cells 24 hr postinoculation. When the glycosylation inhibitor tunicamycin was present (from 0 hr postinoculation) there was no detectable glycosylation of any of these viral-induced glycoproteins. Metabolic labeling of the nonoccluded virus budded from IPLB-21 and TN-368 with tritiated mannose or N-acetylglucosamine identified 11 structural glycoproteins, 8 of which were identical in both virus preparations. All of these structural glycoproteins were sensitive to the inhibitory action of tunicamycin. A single 42K structural glycoprotein was detected (with acetylglucosamine only) in the occluded form of AcNPV. Glycosylation of this structural protein appeared to be insensitive to tunicamycin. Lactoperoxidase-catalyzed radioiodination was used to determine which of the virus structural glycoproteins are exposed on the virion surface.

References

  1. Bächi T., Deas J.E., Howe C. Virus-erythrocyte membrane interactions. In: Poste G., Nicolson G.T., editors. Virus Infection and the Cell Surface. North-Holland; Amsterdam: 1977. pp. 83–127. [Google Scholar]
  2. Burand J.P., Stiles B., Wood H.A. Structural and intracellular proteins of the non-occluded baculovirus Hz-1. J. Virol. 1983;46:137–142. doi: 10.1128/jvi.46.1.137-142.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Butters T.D., Hughes R.C., Vischer P. Steps in the biosynthesis of mosquito cell membrane glycoproteins and the effects of tunicamycin. Biochim. Biophys. Acta. 1981;640:672–686. doi: 10.1016/0005-2736(81)90097-3. [DOI] [PubMed] [Google Scholar]
  4. Carstens E.B., Tjia S.T., Doerfler W. Infection of Spodoptera frugiperda cells with Autographa californica nuclear polyhedrosis virus. Virology. 1979;99:386–398. doi: 10.1016/0042-6822(79)90017-5. [DOI] [PubMed] [Google Scholar]
  5. Dobos P., Cochran M.A. Protein synthesis in cells infected by Autographa californica nuclear polyhedrosis virus (AcNPV): The effect of cytosine arabinoside. Virology. 1980;103:446–464. doi: 10.1016/0042-6822(80)90203-2. [DOI] [PubMed] [Google Scholar]
  6. Etchison J.R., Robertson J.S., Summers D.F. Host cell-dependent differences in the oligosaccharide moieties of the VSV G protein. J. Gen. Virol. 1981;57:43–52. doi: 10.1099/0022-1317-57-1-43. [DOI] [PubMed] [Google Scholar]
  7. Goldstein N.I., McIntosh A.H. Glycoproteins of nuclear polyhedrosis viruses. Archiv. Virol. 1980;64:119–126. doi: 10.1007/BF01318015. [DOI] [PubMed] [Google Scholar]
  8. Hink W.F. Established insect cell line from the cabbage looper, Trichoplusia ni. Nature (London) 1970;226:466–467. doi: 10.1038/226466b0. [DOI] [PubMed] [Google Scholar]
  9. Holmes K.V., Doller E.W., Sturman L.S. Tunicamycin resistant glycosylation of a coronavirus glycoprotein: Demonstration of a novel type of viral glycoprotein. Virology. 1981;115:334–344. doi: 10.1016/0042-6822(81)90115-X. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Huang R.T.C., Rott R., Wahn K., Klenk H.-D., Kohama T. The function of the neuraminidase in membrane fusion induced by myxoviruses. Virology. 1980;107:313–319. doi: 10.1016/0042-6822(80)90299-8. [DOI] [PubMed] [Google Scholar]
  11. Hubbard A.L., Cohn Z.A. The enzymatic iodination of the red cell membrane. J. Cell Biol. 1972;55:390–405. doi: 10.1083/jcb.55.2.390. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Hubbard S.C., Ivatt R.J. Synthesis and processing of asparagine-linked oligosaccharides. Annu. Rev. Biochem. 1981;50:555–583. doi: 10.1146/annurev.bi.50.070181.003011. [DOI] [PubMed] [Google Scholar]
  13. Keegstra K., Burke D. Comparison of the carbohydrate of sindbis virus glycoproteins with carbohydrate of host glycoproteins. J. Supramol. Struct. 1977;7:371–379. doi: 10.1002/jss.400070309. [DOI] [PubMed] [Google Scholar]
  14. Kelly D.C., Lescott T. Baculovirus replication: protein synthesis in Spodoptera frugiperda cells infected with Trichoplusia ni nuclear polyhedrosis virus. Microbiologica (Bologna) 1981;4:35–57. [Google Scholar]
  15. Klenk H.-D., Caliguiri L.A., Choppin P.W. The proteins of the parainfluenza virus SV5, II. The carbohydrate content and glycoproteins of the virion. Virology. 1970;42:473–481. doi: 10.1016/0042-6822(70)90290-4. [DOI] [PubMed] [Google Scholar]
  16. Krebs K.G., Heusser D., Wimmer H. Spray reagents. In: Stahl E., editor. Thin Layer Chromatography. Springer-Verlag; New York/Berlin: 1969. p. 899. [Google Scholar]
  17. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 1970;227:680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  18. Lenard J., Miller D.K. Uncoating of enveloped viruses. Cell. 1982;28:5–6. doi: 10.1016/0092-8674(82)90368-3. [DOI] [PubMed] [Google Scholar]
  19. Little S.P., Jofre J.T., Courtney R.J., Schaffer P.A. A virion associated glycoprotein essential for infectivity of herpes simplex virus type 1. Virology. 1981;115:149–160. doi: 10.1016/0042-6822(81)90097-0. [DOI] [PubMed] [Google Scholar]
  20. Markwell M.A.K., Haas S.M., Tolbert N.E., Bieber L.L. Protein determination in membrane and lipoprotein samples: manual and automated procedures. Methods Enzymol. 1981;72:296–303. doi: 10.1016/s0076-6879(81)72018-4. [DOI] [PubMed] [Google Scholar]
  21. Maruniak J.E. University of Texas; Austin: 1979. Biochemical Characterization of Baculovirus Structural and Infected TN-368 Cell Polypeptides, Glycoproteins, and Phosphoproteins. (Ph.D. Thesis). [Google Scholar]
  22. Maruniak J.E., Summers M.D. Autographa californica nuclear polyhedrosis virus phosphoproteins and synthesis of intracellular proteins after virus infection. Virology. 1981;109:25–34. doi: 10.1016/0042-6822(81)90468-2. [DOI] [PubMed] [Google Scholar]
  23. Niemann H., Klenk H.-D. Coronavirus glycoprotein E1, a new type of viral glycoprotein. J. Mol. Biol. 1981;153:993–1010. doi: 10.1016/0022-2836(81)90463-0. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Patzer E.J., Wagner R.R., Dubovi E.J. Viral membranes: model systems for studying biological membranes. CRC Crit. Rev. Biochem. 1979;6:165–217. doi: 10.3109/10409237909102563. [DOI] [PubMed] [Google Scholar]
  25. Payne L.G., Kristensson K. Effect of glycosylation inhibitors on the release of enveloped vaccinia virus. J. Virol. 1982;41:367–375. doi: 10.1128/jvi.41.2.367-375.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Roth M.G., Fitzpatrick J.P., Compans R.W. Vol. 76. 1979. Polarity of influenza and vesicular stomatitis virus maturation in MDCK cells: lack of a requirement for glycosylation of viral proteins; pp. 6430–6434. (Proc. Natl. Acad. Sci. USA). [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Shida H., Dales S. Biogenesis of vaccinia: Carbohydrate of the hemagglutinin molecule. Virology. 1981;111:56–72. doi: 10.1016/0042-6822(81)90653-x. [DOI] [PubMed] [Google Scholar]
  28. Simons K., Garoff H. The budding mechanisms of enveloped animal viruses. J. Gen. Virol. 1980;50:1–21. doi: 10.1099/0022-1317-50-1-1. [DOI] [PubMed] [Google Scholar]
  29. Stiles B., Wood H.A., Hughes P.R. Effect of tunicamycin on the infectivity of Autographa californica nuclear polyhedrosis virus. J. Invertebr. Pathol. 1983;41:405–408. [Google Scholar]
  30. Stiles B., Burand J.P., Meda M., Wood H.A. Characterization of the Gypsy moth (Lymantria dispar) nuclear polyhedrosis virus. Appl. Environ. Microbiol. 1983;46:297–307. doi: 10.1128/aem.46.2.297-303.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Stohrer R., Hunter E. Inhibition of Rous sarcoma virus replication by 2-deoxyglucose and tunicamycin: identification of an unglycosylated envelope gene product. J. Virol. 1979;32:412–419. doi: 10.1128/jvi.32.2.412-419.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Summers M.D., Smith G.E. Baculovirus structural polypeptides. Virology. 1978;84:390–402. doi: 10.1016/0042-6822(78)90257-x. [DOI] [PubMed] [Google Scholar]
  33. Svennerholm B., Olofsson S., Lundén R., Vahlne A., Lycke E. Adsorption and penetration of enveloped herpes simplex virus particles modified by tunicamycin or 2-deoxy-D-glucose. J. Gen. Virol. 1982;63:343–349. doi: 10.1099/0022-1317-63-2-343. [DOI] [PubMed] [Google Scholar]
  34. Takatsuki A., Tamura G. Inhibition of glycoconjugate biosynthesis by tunicamycin. In: Tamura G., editor. Tunicamycin. Japan Scientific Societies Press; Tokyo: 1982. [Google Scholar]
  35. Wood H.A. An agar overlay plaque assay method for Autographa californica nuclear polyhedrosis virus. J. Invertebr. Pathol. 1977;29:304–307. [Google Scholar]
  36. Wood H.A. Autographa californica nuclear polyhedrosis virus-induced proteins in tissue culture. Virology. 1980;102:21–27. doi: 10.1016/0042-6822(80)90066-5. [DOI] [PubMed] [Google Scholar]
  37. Wood H.A. Protease degradation of Autographia californica nuclear polyhedrosis virus proteins. Virology. 1980;103:392–399. doi: 10.1016/0042-6822(80)90198-1. [DOI] [PubMed] [Google Scholar]

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