Transport of vesicular stomatitis virus glycoprotein in a cell-free extract (original) (raw)

Abstract

We describe a cell-free system in which the membrane glycoprotein of vesicular stomatitis virus is rapidly and efficiently transported to membranes of the Golgi complex by a process resembling intracellular protein transport. Transport in vitro is energy-dependent and is accompanied by terminal glycosylation of the membrane glycoprotein (dependent upon UDP-GlcNAc and resulting in resistance to endo-beta-N-acetylglucosaminidase H).

3870

Images in this article

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Gottlieb C., Baenziger J., Kornfeld S. Deficient uridine diphosphate-N-acetylglucosamine:glycoprotein N-acetylglucosaminyltransferase activity in a clone of Chinese hamster ovary cells with altered surface glycoproteins. J Biol Chem. 1975 May 10;250(9):3303–3309. [PubMed] [Google Scholar]
  2. Jamieson J. D., Palade G. E. Intracellular transport of secretory proteins in the pancreatic exocrine cell. IV. Metabolic requirements. J Cell Biol. 1968 Dec;39(3):589–603. doi: 10.1083/jcb.39.3.589. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Katz F. N., Lodish H. F. Transmembrane biogenesis of the vesicular stomatitis virus glycoprotein. J Cell Biol. 1979 Feb;80(2):416–426. doi: 10.1083/jcb.80.2.416. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Knipe D. M., Baltimore D., Lodish H. F. Separate pathways of maturation of the major structural proteins of vesicular stomatitis virus. J Virol. 1977 Mar;21(3):1128–1139. doi: 10.1128/jvi.21.3.1128-1139.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Knipe D. M., Lodish H. F., Baltimore D. Localization of two cellular forms of the vesicular stomatitis viral glycoprotein. J Virol. 1977 Mar;21(3):1121–1127. doi: 10.1128/jvi.21.3.1121-1127.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  7. Lenard J. Virus envelopes and plasma membranes. Annu Rev Biophys Bioeng. 1978;7:139–165. doi: 10.1146/annurev.bb.07.060178.001035. [DOI] [PubMed] [Google Scholar]
  8. Li E., Kornfeld S. Structure of the altered oligosaccharide present in glycoproteins from a clone of Chinese hamster ovary cells deficient in N-acetylglucosaminyltransferase activity. J Biol Chem. 1978 Sep 25;253(18):6426–6431. [PubMed] [Google Scholar]
  9. Narasimhan S., Stanley P., Schachter H. Control of glycoprotein synthesis. Lectin-resistant mutant containing only one of two distinct N-acetylglucosaminyltransferase activities present in wild type Chinese hamster ovary cells. J Biol Chem. 1977 Jun 10;252(11):3926–3933. [PubMed] [Google Scholar]
  10. Palade G. Intracellular aspects of the process of protein synthesis. Science. 1975 Aug 1;189(4200):347–358. doi: 10.1126/science.1096303. [DOI] [PubMed] [Google Scholar]
  11. Robbins P. W., Hubbard S. C., Turco S. J., Wirth D. F. Proposal for a common oligosaccharide intermediate in the synthesis of membrane glycoproteins. Cell. 1977 Dec;12(4):893–900. doi: 10.1016/0092-8674(77)90153-2. [DOI] [PubMed] [Google Scholar]
  12. Rothman J. E., Fine R. E. Coated vesicles transport newly synthesized membrane glycoproteins from endoplasmic reticulum to plasma membrane in two successive stages. Proc Natl Acad Sci U S A. 1980 Feb;77(2):780–784. doi: 10.1073/pnas.77.2.780. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Rothman J. E., Katz F. N., Lodish H. F. Glycosylation of a membrane protein is restricted to the growing polypeptide chain but is not necessary for insertion as a transmembrane protein. Cell. 1978 Dec;15(4):1447–1454. doi: 10.1016/0092-8674(78)90068-5. [DOI] [PubMed] [Google Scholar]
  14. Schachter H., Jabbal I., Hudgin R. L., Pinteric L., McGuire E. J., Roseman S. Intracellular localization of liver sugar nucleotide glycoprotein glycosyltransferases in a Golgi-rich fraction. J Biol Chem. 1970 Mar 10;245(5):1090–1100. [PubMed] [Google Scholar]
  15. Schlesinger S., Gottlieb C., Feil P., Gelb N., Kornfeld S. Growth of enveloped RNA viruses in a line of chinese hamster ovary cells with deficient N-acetylglucosaminyltransferase activity. J Virol. 1975 Jan;17(1):239–246. doi: 10.1128/jvi.17.1.239-246.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Tabas I., Kornfeld S. Purification and characterization of a rat liver Golgi alpha-mannosidase capable of processing asparagine-linked oligosaccharides. J Biol Chem. 1979 Nov 25;254(22):11655–11663. [PubMed] [Google Scholar]
  17. Tabas I., Kornfeld S. The synthesis of complex-type oligosaccharides. III. Identification of an alpha-D-mannosidase activity involved in a late stage of processing of complex-type oligosaccharides. J Biol Chem. 1978 Nov 10;253(21):7779–7786. [PubMed] [Google Scholar]
  18. Tartakoff A. M., Vassalli P. Plasma cell immunoglobulin secretion: arrest is accompanied by alterations of the golgi complex. J Exp Med. 1977 Nov 1;146(5):1332–1345. doi: 10.1084/jem.146.5.1332. [DOI] [PMC free article] [PubMed] [Google Scholar]