Virus-cell binding inhibitors

Sulphated PS, potent antiviral agents, were also evaluated in vitro as inhibitors of influenza virus replication [119], The fact that the sulphated PS are inhibitory to some myxoviruses and retroviruses but not to others seems to depend on the composition of the amino acid sequences of the viral envelope glycoproteins that are involved in virus-cell binding and fusion [120],... 

Viral Inhibitors. A multivalency approach was used to inhibit influenza virus in-fectivity. Several sialic acid-based polymers have been synthesized that inhibit flu virus receptor-binding activity, which in turn impedes flu viruses from sticking to cell surfaces and subsequent viral infection of cells (see also Section 2.1.4) (155,156). 

Multi- and polyvalent interactions between lectins and glycans are of fundamental importance for the interaction of biological surfaces. Lectins are proteins with defined glycan-recognition domains on the surface of viruses and bacteria as well as of plant and animal cells. Affine inhibitors of lectins are, therefore, suitable for clarifying the function of defined carbohydrate stmctures, when they are used as a competitive binding partner. They also provide an opportunity for pharmacological intervention. The phenomenon of... 

The influenza virus inhibitors, zanamivir, and oseltamivir, act outside the cell after virus particles have been formed. The dtugs have been designed to fit into the active site of the viral envelope enzyme neuraminidase, which is required to cleave sialic acid off the surface of the producing cells. When its activity is blocked, new virus particles stay attached to the cell surface through binding of the virus protein hemagglutinin to sialic acid and are prevented from spreading to other cells. 

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