Disulfide bonds in Sendai virus glycoproteins

J. M. Hardwick, R. H. Bussell

Research output: Contribution to journalArticlepeer-review

Abstract

The precursor of fusion protein (F0) in Sendai virus grown in Vero cells can be cleaved by trypsin to forms F1 and F2, which can be resolved on SDS-polyacrylamide gels. However, if disulfide bonds are preserved during electrophoresis, F1 and F2 remain linked together even after trysin treatment (F). Sendai virus grown in embryonated chicken eggs does not contain the precursor F0. However, an F protein was found for Sendai virus grown in eggs when disulfide bonds were preserved during electrophoresis. The hemagglutinin-neuraminidase (HN) glyco-proteins also appear to be disulfide-linked to form large complexes which are observed on SDS-polyacrylamide gels of nonreduced samples.

Original languageEnglish (US)
Pages (from-to)300-306
Number of pages7
JournalIntervirology
Volume11
Issue number5
DOIs
StatePublished - Jan 1 1979
Externally publishedYes

ASJC Scopus subject areas

  • Virology
  • Infectious Diseases

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