Sulfated components of enveloped viruses

A. Pinter, R. W. Compans

Research output: Contribution to journalArticlepeer-review

26 Scopus citations

Abstract

The glycoproteins of several enveloped viruses, grown in a variety of cell types, are labeled with 35SO4-2, whereas the nonglycosylated proteins are not. This was shown for the HN and F glycoproteins of SV5 and Sendai virus, the E1 and E2 glycoproteins of Sindbis virus, and for the major glycoprotein gp69, as well as for a minor glycoprotein, gp52, of Rauscher leukemia virus. The minor glycoprotein of Rauscher leukemia virus is more highly sulfated, with a ratio of 35SO4- [3H]glucosamine about threefold greater than that of gp69. The G protein of vesicular stomatitis virus was labeled when virions were grown in the MDBK line of bovine kidney cells, although no significant incorporation of 35SO4-2 into this protein was observed in virions grown in BHK21 F line of baby hamster kidney cells. In addition to the viral glycoproteins, sulfate was also incorporated into a heterogeneous component with an electrophoretic mobility lower than that of any of the viral proteins in polyacrylamide gel electrophoresis. For virions doubly labeled with 35SO4-2 and [3H]leucine, this component had a much greater 35S 3H ratio than any of the viral polypeptides and thus could not represent aggregated viral proteins. This material is believed to be a cell derived mucopolysaccharide and can be removed from virions by treatment with hyaluronidase without affecting the amount of sulfate present on the glycoproteins.

Original languageEnglish (US)
Pages (from-to)859-866
Number of pages8
JournalJournal of virology
Volume16
Issue number4
DOIs
StatePublished - 1975
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Insect Science
  • Virology
  • Microbiology
  • Immunology

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