The Purification and Structural Characterization of the Fusion Factor of Sendai Virus
The fusion factor (F) and the hemagglutinin-neuraminidase (HN) of Sendai virus have been purified by lectin affinity chromatography on a Lens culimris (LcH)-Sepharose column. Separation was achieved by sequential elution with two different detergents containing a methyl mannoside. HN was eluted with the zwitterionic detergent Empigen BB and F with the anionic detergent sodium deoxycholate. F was further purified by molecular sieving on Ultrogel AcA34 and separated into its two component chains (F1 apparent M.W. 53,000 and F2 apparent M.W. 15,000) by molecular sieving on Sephadex G-100 after reduction of disulfide bonds. The amino terminus of F1 was PHE-PHE-GLY-ALA-VAL-ILE-GLY-ILEILE-ALA-. This sequence shows identity at six positions with the amino terminal sequence of the small polypeptide chain (HA2) of the influenza virus hemagglutinin. The amino terminal ten residues of F1 and HA2 are extremely hydrophobic and are both generated by proteolytic cleavage of an inactive precursor polypeptide. Structure and function correlations of this cleavage are discussed.
KeywordsCyanogen Bromide Sendai Virus Fusion Activity Galactose Oxidase Influenza Virus Hemagglutinin
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- WATERFIELD, M. D., SKEHEL, J. J., NAKASHIMA, Y., GURNETT, A. and BILHAM, T.(1977)this volume.Google Scholar