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Purification of the Fusion Protein of Sendai Virus: Analysis of the NH2-Terminal Sequence Generated during Precursor Activation
M. J. Gething, J. M. White and M. D. Waterfield
Proceedings of the National Academy of Sciences of the United States of America
Vol. 75, No. 6 (Jun., 1978), pp. 2737-2740
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/68317
Page Count: 4
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The two glycoproteins of Sendai virus, the hemagglutinin-neuraminidase and the fusion protein (F), were separated and purified by affinity chromatography on a Lens culinaris lectin-Sepharose column. F was shown to consist of two disulfide-bonded glycopolypeptide chains, F1 and F2, of molecular weights 51,000 and 11,000, each of which contained 15% carbohydrate by weight. Amino-terminal sequence analysis showed that F2 was blocked and that the hydrophobic sequence NH2-Phe-Phe-Gly-Ala-Val-Ile-Gly-Ile-Ile-Ala-Leu-Gly-Pro-Ala-Thr- was at the amino terminus of F1. This sequence shows identity at six positions with the hydrophobic amino-terminal sequence of the smaller glycopolypeptide chain, HA2, of the hemagglutinin of influenza virus. Both F1 and HA2 are formed by proteolytic cleavage of precursor glycoproteins (F0, Sendai virus; HA0, influenza virus). Since these cleavages confer infectivity upon both Sendai and influenza viruses and the ability to induce cell-to-cell fusion upon Sendai virus, the hydrophobic NH2-terminal sequences on F1 and HA2 may play a role in fusion of viral and host-cell membranes.
Proceedings of the National Academy of Sciences of the United States of America © 1978 National Academy of Sciences