Disruption of myxoviruses with Tween 20 and isolation of biologically active hemagglutinin and neuraminidase subunits.

Myxoviruses were disrupted with Tween 20 at high pH, and the major surface antigens were separated in biologically active form. The neuraminidase had a sedimentation coefficient of 10.8S, and the hemagglutinin had a sedimentation coefficient of 8.1S. Electron microscopic examination of negatively stained preparations revealed structures identical in size and morphology to the neuraminidase and hemagglutinin subunits described by others. Inhibition of neuraminidase activity by antibody to the hemagglutinin which occurred with intact viruses (probably for "steric" reasons) did not occur after the viruses were disrupted with Tween 20. Serological assays for neuraminidase were possible in the presence of the mild surfactant, whereas serological assays for hemagglutinin were possible after removal of the reagent. Disruption of myxoviruses with Tween 20 therefore provides a method for the independent study of these antigens during antigenic drift.