Abstract
The identity of the glycoprotein of vesicular stomatitis virus (VSV) as the spike protein has been confirmed by the removal of the spikes with a protease from Streptomyces griseus, leaving bullet-shaped particles bounded by a smooth membrane. This treatment removes the glycoprotein but does not affect the other virion proteins, apparently because they are protected from the enzyme by the lipids in the viral membrane. The proteins of phenotypically mixed, bullet-shaped virions produced by cells mixedly infected with VSV and the parainfluenza virus simian virus 5 (SV5) have been analyzed by polyacrylamide gel electrophoresis. These virions contain all the VSV proteins plus the two SV5 spike proteins, both of which are glycoproteins. The finding of the SV5 spike glycoproteins on virions with the typical morphology of VSV indicates that there is not a stringent requirement that only the VSV glycoprotein can be used to form the bullet-shaped virion. On the other hand, the SV5 nucleocapsid protein and the major non-spike protein of the SV5 envelope were not detected in the phenotypically mixed virions, and this suggests that a specific interaction between the VSV nucleocapsid and regions of the cell membrane which contain the nonglycosylated VSV envelope protein is necessary for assembly of the bullet-shaped virion.
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Selected References
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- BABLANIAN R., EGGERS H. J., TAMM I. STUDIES ON THE MECHANISM OF POLIOVIRUS-INDUCED CELL DAMAGE. I. THE RELATION BETWEEN POLIOVIRUS,-INDUCED METABOLIC AND MORPHOLOGICAL ALTERATIONS IN CULTURED CELLS. Virology. 1965 May;26:100–113. doi: 10.1016/0042-6822(65)90030-9. [DOI] [PubMed] [Google Scholar]
- Burge B. W., Huang A. S. Comparison of membrane protein glycopeptides of Sindbis virus and vesicular stomatitis virus. J Virol. 1970 Aug;6(2):176–182. doi: 10.1128/jvi.6.2.176-182.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
- CHOPPIN P. W. MULTIPLICATION OF A MYXOVIRUS (SV5) WITH MINIMAL CYTOPATHIC EFFECTS AND WITHOUT INTERFERENCE. Virology. 1964 Jun;23:224–233. doi: 10.1016/0042-6822(64)90286-7. [DOI] [PubMed] [Google Scholar]
- Caliguiri L. A., Klenk H. D., Choppin P. W. The proteins of the parainfluenza virus SV5. 1. Separation of virion polypeptides by polyacrylamide gel electrophoresis. Virology. 1969 Nov;39(3):460–466. doi: 10.1016/0042-6822(69)90094-4. [DOI] [PubMed] [Google Scholar]
- Cartwright B., Talbot P., Brown F. The proteins of biologically active sub-units of vesicular stomatitis virus. J Gen Virol. 1970 Jun;7(3):267–272. doi: 10.1099/0022-1317-7-3-267. [DOI] [PubMed] [Google Scholar]
- Chen C., Compans R. W., Choppin P. W. Parainfluenza virus surface projections: glycoproteins with haemagglutinin and neuraminidase activities. J Gen Virol. 1971 Apr;11(1):53–58. doi: 10.1099/0022-1317-11-1-53. [DOI] [PubMed] [Google Scholar]
- Choppin P. W., Compans R. W. Phenotypic mixing of envelope proteins of the parainfluenza virus SV5 and vesicular stomatitis virus. J Virol. 1970 May;5(5):609–616. doi: 10.1128/jvi.5.5.609-616.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Choppin P. W. Replication of influenza virus in a continuous cell line: high yield of infective virus from cells inoculated at high multiplicity. Virology. 1969 Sep;39(1):130–134. doi: 10.1016/0042-6822(69)90354-7. [DOI] [PubMed] [Google Scholar]
- Compans R. W., Klenk H. D., Caliguiri L. A., Choppin P. W. Influenza virus proteins. I. Analysis of polypeptides of the virion and identification of spike glycoproteins. Virology. 1970 Dec;42(4):880–889. doi: 10.1016/0042-6822(70)90337-5. [DOI] [PubMed] [Google Scholar]
- Compans R. W. Location of the glycoprotein in the membrane of Sindbis virus. Nat New Biol. 1971 Jan 27;229(4):114–116. doi: 10.1038/newbio229114a0. [DOI] [PubMed] [Google Scholar]
- Igarashi A., Fukuoka T., Nithiuthai P., Hsu L. C., Fukai K. Structural components of chikungunya virus. Biken J. 1970 Jun;13(2):93–110. [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]
- Kang C. Y., Prevec L. Proteins of vesicular stomatitis virus. II. Immunological comparisons of viral antigens. J Virol. 1970 Jul;6(1):20–27. doi: 10.1128/jvi.6.1.20-27.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 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 Oct;42(2):473–481. doi: 10.1016/0042-6822(70)90290-4. [DOI] [PubMed] [Google Scholar]
- Klenk H. D., Choppin P. W. Chemical composition of the parainfluenza virus SV5. Virology. 1969 Jan;37(1):155–157. doi: 10.1016/0042-6822(69)90321-3. [DOI] [PubMed] [Google Scholar]
- Klenk H. D., Choppin P. W. Glycolipid content of vesicular stomatitis virus grown in baby hamster kidney cells. J Virol. 1971 Mar;7(3):416–417. doi: 10.1128/jvi.7.3.416-417.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- Maizel J. V., Jr, White D. O., Scharff M. D. The polypeptides of adenovirus. I. Evidence for multiple protein components in the virion and a comparison of types 2, 7A, and 12. Virology. 1968 Sep;36(1):115–125. doi: 10.1016/0042-6822(68)90121-9. [DOI] [PubMed] [Google Scholar]
- McCombs R. M., Melnick M. B., Brunschwig J. P. Biophysical studies of vesicular stomatitis virus. J Bacteriol. 1966 Feb;91(2):803–812. doi: 10.1128/jb.91.2.803-812.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
- McSharry J. J., Wagner R. R. Carbohydrate composition of vesicular stomatitis virus. J Virol. 1971 Mar;7(3):412–415. doi: 10.1128/jvi.7.3.412-415.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
- McSharry J. J., Wagner R. R. Lipid composition of purified vesicular stomatitis viruses. J Virol. 1971 Jan;7(1):59–70. doi: 10.1128/jvi.7.1.59-70.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
- McSharry J., Benzinger R. Concentration and purification of vesicular stomatitis virus by polyethylene glycol "precipitation". Virology. 1970 Mar;40(3):745–746. doi: 10.1016/0042-6822(70)90219-9. [DOI] [PubMed] [Google Scholar]
- Mountcastle W. E., Compans R. W., Caliguiri L. A., Choppin P. W. Nucleocapsid protein subunits of simian virus 5, Newcastle disease virus, and Sendai virus. J Virol. 1970 Nov;6(5):677–684. doi: 10.1128/jvi.6.5.677-684.1970. [DOI] [PMC free article] [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]
- Schulze I. T. The structure of influenza virus. I. The polypeptides of the virion. Virology. 1970 Dec;42(4):890–904. doi: 10.1016/0042-6822(70)90338-7. [DOI] [PubMed] [Google Scholar]
- WARREN L. The thiobarbituric acid assay of sialic acids. J Biol Chem. 1959 Aug;234(8):1971–1975. [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., Schnaitman T. C., Snyder R. M., Schnaitman C. A. Protein composition of the structural components of vesicular stomatitis virus. J Virol. 1969 Jun;3(6):611–618. doi: 10.1128/jvi.3.6.611-618.1969. [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]