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Location of Post-translational Cleavage Events Within F and HN Glycoproteins of Newcastle Disease Virus

Department of Genetics, University of Newcastle upon Tyne, Newcastle upon Tyne NE1 7RU, U.K.

The biologically active form of the fusion glycoprotein F from Newcastle disease virus (NDV) comprises two polypeptides, F₁ and F₂ (derived from a precursor polypeptide F₀ by a post translational cleavage event), which are covalently linked together (F_1,2) by disulphide bonds. This feature was exploited in a two-dimensional SDS-polyacrylamide gel electrophoretic analysis to orientate the position of the cleavage event within F₀. Separation of proteins from NDV-infected CEF in the first dimension in the absence of reducing agent resolved F_1,2 protein from all NDV-induced proteins other than F₀. Reduction of the first dimension gel with 2-mercaptoethanol, followed by electrophoresis in the second dimension, resolved F₁ (55K), F₂ (12.5K) and F₀ (64K) proteins. The only polypeptides other than F₁ and F₂ which fell below the diagonal, indicating the positions of the polypeptides from infected cells, were two minor glycoproteins designated HN₁ (51.5K) and HN₂ (27.5K) which took up positions vertically beneath the major haemagglutinin-neuraminidase glycoprotein HN (75K). Dual isotope labelling experiments with NDV-infected chick embryo fibroblasts, which had previously received a salt shock to effect synchronization of polypeptide initiation upon release of salt shock, revealed the following orientations within the parent molecules: NH₂F₂F₁COOH and NH₂HN₁HN₂COOH.

The existence of intermolecular disulphide bonds, orientation and relative lengths of the two NDV HN fragments is analogous to the HA₁ and HA₂ proteins of influenza virus haemagglutinin.

^* Present address: Department of Biology, University of York, England.

Received 28 June 1979; accepted 25 September 1979.