Abstract
All five major viral proteins were synthesized in chicken embryo cells infected with vesicular stomatitis virus temperature-sensitive (ts) mutants of complementation groups III and V and maintained at the nonpermissive temperature. The distribution of these proteins among cytoplasmic cellular fractions separated on discontinuous sucrose gradients was identical for wild-type and tsIII-infected cells. Strikingly different patterns were observed for the G protein in gradients from cells infected by tsV mutants; very little, if any, G protein was found in the lightest fraction. Pulse and chase experiments with wild-type, virus-infected cells showed that protein G moves from the heaviest to the lightest fraction before being incorporated into the virion. After shift down to the permissive temperature (30 C), G protein synthesized at 39.6 C in tsV-infected cells became associated with the lightest cellular fraction and later with the released virions. In contrast, M protein, synthesized at 39.6 C in tsIII-infected cells, was not incorporated into the virions after shift down. These data strongly suggest, first, that M protein is encoded by the vesicular stomatitis gene III, and second, that incorporation of G protein in the lightest cellular fraction is a necessary step of vesicular stomatitis maturation. This step is impaired by tsV mutations.
Full text
PDF![1220](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c0ae/355638/43c0f5bf2e14/jvirol00251-0214.png)
![1221](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c0ae/355638/69cde617239f/jvirol00251-0215.png)
![1222](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c0ae/355638/ed2e89afe83e/jvirol00251-0216.png)
![1223](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c0ae/355638/d08e5a1b3a4e/jvirol00251-0217.png)
![1224](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c0ae/355638/3a5be459ddeb/jvirol00251-0218.png)
![1225](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c0ae/355638/d295dd84210d/jvirol00251-0219.png)
![1226](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c0ae/355638/754ee33e4b79/jvirol00251-0220.png)
![1227](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c0ae/355638/6440ae971af0/jvirol00251-0221.png)
![1228](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c0ae/355638/3667b3304f9f/jvirol00251-0222.png)
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Bishop D. H., Roy P. Dissociation of vesicular stomatitis virus and relation of the virion proteins to the viral transcriptase. J Virol. 1972 Aug;10(2):234–243. doi: 10.1128/jvi.10.2.234-243.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Caliguiri L. A., Tamm I. The role of cytoplasmic membranes in poliovirus biosynthesis. Virology. 1970 Sep;42(1):100–111. doi: 10.1016/0042-6822(70)90242-4. [DOI] [PubMed] [Google Scholar]
- Cartwright B. The distribution of virus proteins in BHK 21 cells infected with vesicular stomatitis virus (Indiana C). J Gen Virol. 1973 Nov;21(2):407–411. doi: 10.1099/0022-1317-21-2-407. [DOI] [PubMed] [Google Scholar]
- Cohen G. H., Atkinson P. H., Summers D. F. Interactions of vesicular stomatitis virus structural proteins with HeLa plasma membranes. Nat New Biol. 1971 May 26;231(21):121–123. doi: 10.1038/newbio231121a0. [DOI] [PubMed] [Google Scholar]
- Cohen G. H., Summers D. F. In vitro association of vesicular stomatitis virus proteins with purified HeLa and erythrocyte plasma membranes. Virology. 1974 Feb;57(2):566–569. doi: 10.1016/0042-6822(74)90195-0. [DOI] [PubMed] [Google Scholar]
- Compans R. W. Influenza virus proteins. II. Association with components of the cytoplasm. Virology. 1973 Jan;51(1):56–70. doi: 10.1016/0042-6822(73)90365-6. [DOI] [PubMed] [Google Scholar]
- David A. E. Assembly of the vesicular stomatitis virus envelope: incorporation of viral polypeptides into the host plasma membrane. J Mol Biol. 1973 May 5;76(1):135–148. doi: 10.1016/0022-2836(73)90085-5. [DOI] [PubMed] [Google Scholar]
- Deutsch V., Berkaloff A. Analyse d'un mutant thermolabile du virus de la stomatite vésiculaire (VSV. Ann Inst Pasteur (Paris) 1971 Jul;121(1):101–106. [PubMed] [Google Scholar]
- Flamand A. Etude génétique du virus de la stomatite vésiculaire: classement de mutants thermosensibles spontanés en groupes de complémentation. J Gen Virol. 1970 Sep;8(3):187–195. doi: 10.1099/0022-1317-8-3-187. [DOI] [PubMed] [Google Scholar]
- Flamand A., Pringle C. R. The homologies of spontaneous and induced temperature-sensitive mutants of vesicular stomatitis virus isolated in chick embryo and BHK 21 cells. J Gen Virol. 1971 May;11(2):81–85. doi: 10.1099/0022-1317-11-2-81. [DOI] [PubMed] [Google Scholar]
- Kang C. Y., Prevec L. Proteins of vesicular stomatitis virus. 3. Intracellular synthesis and extracellular appearance of virus-specific proteins. Virology. 1971 Dec;46(3):678–690. doi: 10.1016/0042-6822(71)90070-5. [DOI] [PubMed] [Google Scholar]
- Kang C. Y., Prevec L. Proteins of vesicular stomatitis virus. I. Polyacrylamide gel analysis of viral antigens. J Virol. 1969 Apr;3(4):404–413. doi: 10.1128/jvi.3.4.404-413.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Klenk H. D., Wöllert W., Rott R., Scholtissek C. Association of influenza virus proteins with cytoplasmic fractions. Virology. 1974 Jan;57(1):28–41. doi: 10.1016/0042-6822(74)90105-6. [DOI] [PubMed] [Google Scholar]
- Lafay F., Berkaloff A. Etude des mutants thermosensibles du virus de la stomatite vésiculaire (VSV). Mutants de maturation. C R Acad Sci Hebd Seances Acad Sci D. 1969 Sep 15;269(11):1031–1034. [PubMed] [Google Scholar]
- Lafay F. Etude des fonctions du virus de la stomatite vésiculaire altérées par une mutation thermosensible: mise en evidence dela protéine structurale affectée par la mutation ts 23. J Gen Virol. 1971 Dec;13(3):449–453. doi: 10.1099/0022-1317-13-3-449. [DOI] [PubMed] [Google Scholar]
- Lafay F. Etude des mutants thermosensibles du Virus de la Stomatite Vésiculaire (VSV). Classification de quelques mutants d'après des critères de fonctionnement. C R Acad Sci Hebd Seances Acad Sci D. 1969 May 12;268(19):2385–2388. [PubMed] [Google Scholar]
- Maizel J. V., Jr Acrylamide-gel electrophorograms by mechanical fractionation: radioactive adenovirus proteins. Science. 1966 Feb 25;151(3713):988–990. doi: 10.1126/science.151.3713.988. [DOI] [PubMed] [Google Scholar]
- Mudd J. A., Summers D. F. Protein synthesis in vesicular stomatitis virus-infected HeLa cells. Virology. 1970 Oct;42(2):328–340. doi: 10.1016/0042-6822(70)90277-1. [DOI] [PubMed] [Google Scholar]
- Obijeski J. F., Simpson R. W. Conditional lethal mutants of vesicular stomatitis virus. II. Synthesis of virus-specific polypeptides in nonpermissive cells infected with "RNA-" host-restricted mutants. Virology. 1974 Feb;57(2):369–377. doi: 10.1016/0042-6822(74)90176-7. [DOI] [PubMed] [Google Scholar]
- Printz P., Wagner R. R. Temperature-sensitive mutants of vesicular stomatitis virus: synthesis of virus-specific proteins. J Virol. 1971 May;7(5):651–662. doi: 10.1128/jvi.7.5.651-662.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Wagner R. R., Kiley M. P., Snyder R. M., Schnaitman C. A. Cytoplasmic compartmentalization of the protein and ribonucleic acid species of vesicular stomatitis virus. J Virol. 1972 Apr;9(4):672–683. doi: 10.1128/jvi.9.4.672-683.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Wagner R. R., Prevec L., Brown F., Summers D. F., Sokol F., MacLeod R. Classification of rhabdovirus proteins: a proposal. J Virol. 1972 Dec;10(6):1228–1230. doi: 10.1128/jvi.10.6.1228-1230.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Wagner R. R., Schnaitman T. A., Snyder R. M. Structural proteins of vesicular stomatitis viruses. J Virol. 1969 Apr;3(4):395–403. doi: 10.1128/jvi.3.4.395-403.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Wagner R. R., Snyder R. M., Yamazaki S. Proteins of vesicular stomatitis virus: kinetics and cellular sites of synthesis. J Virol. 1970 May;5(5):548–558. doi: 10.1128/jvi.5.5.548-558.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Wong P. K., Holloway A. F., Cormack D. V. Characterization of three complementation groups of vesicular stomatitis virus. Virology. 1972 Dec;50(3):829–840. doi: 10.1016/0042-6822(72)90437-0. [DOI] [PubMed] [Google Scholar]