Fusion of Sendai virus with liposome depends on only F protein, but not HN protein

Sendai virus is able to fuse with liposomes even without virus receptors. To determine the roles of envelope protein, hemagglutinin-neuraminidase (HN) and fusion (F) protein, in Sendai virus-liposome fusion, we treated the virus with proteases and examined its fusion with liposomes and the conditions of HN and F protein. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and western blotting analysis showed that the virus treated with 150 units/ml of trypsin, which inactivated selectively hemolysis activity, maintained intact HN, F and partially digested F (32 kDa) protein, while virus treated with 15,000 units/ml of trypsin, which inactivated both hemolysis and neuraminidase activity, had only a 15-kDa digested HN protein and completely digested F protein. The former fused with liposomes, but the latter did not. In the virus treated with chymotrypsin, which lost both hemolysis and neuraminidase activity, F protein was intact, while HN protein was degraded to 15 kDa; in this case the virus fused with liposomes. As the virus with 15-kDa HN protein fused with liposomes and that with 20-kDa protein did not, HN protein does not appear to play any role in virus-liposome fusion. The virus that fused with liposomes had intact F protein. We conclude that Sendai virus-liposome fusion is strongly dependent on the presence of intact F protein, but not HN protein.