Disulfide bonds in Sendai virus glycoproteins

J. M. Hardwick; R. H. Bussell

doi:10.1159/000149049

Disulfide bonds in Sendai virus glycoproteins

Research output: Contribution to journal › Article › peer-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 language	English (US)
Pages (from-to)	300-306
Number of pages	7
Journal	Intervirology
Volume	11
Issue number	5
DOIs	https://doi.org/10.1159/000149049
State	Published - Jan 1 1979
Externally published	Yes

ASJC Scopus subject areas

Virology
Infectious Diseases

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AB - 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.

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Disulfide bonds in Sendai virus glycoproteins

Abstract

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