Tethered Neuraminidase Inhibitors That Bind an Influenza Virus: A First Step Towards a Diagnostic Method for Influenza

摘要

Influenza viruses are isolated as mall (80 to 120 nm diameter), generally spherical particles. The lipid bilayer envelope of the virus is derived from the host cell and protruding from this membrane on the surface of the virus are two virus-encoded glycoproteins, hemagglutinin (HA) and neuraminidase (NA). HA is the major surface antigen of the virus and is responsible for the binding of virions to the receptors of the host cell and for fusion between the virion envelope and the host cell. NA, the minor surface antigen, is a glycosidase that cleaves sialic acid, 1 (N-acetylneuraminic acid) from the terminal position of glycoproteins and it is thought to be important for the release of virions from the surface of the host cell, and possibly also enhances infectivity by allowing movement of the virus through the mucins lining the respiratory tract. Herein we describe the synthesis of tethered NA inhibitors, which potentially have a high affinity for all strains of influenza A and B, and can be used to capture influenza virions.