Abstract
Flocculation of virions by a viral neuraminidase inhibitor, neuraminin, was examined by low speed centrifugation and electron microscopy. The inhibitor could flocculate virions of influenza viruses but not those of Newcastle disease viruses. Virion-free neuraminidase of influenza virus was also flocculated by this inhibitor. The flocculation was temperature dependent and proceeded rapidly over a wide pH range. The amount of the inhibitor required for complete flocculation of virions was similar to that for the maximum inhibition of neuraminidase. Viral neuraminin receptors were stable to various enzymological, physical, and chemical treatments which caused a loss or reduction of the activity of neuraminidase.
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