Interaction with hemagglutinin

O Keefe, B.R., Smee, D. F., Turpin, J.A., Sau-cedo, C. J., Gustafson, K. R., Mori, T, Blake-slee, D., Buckheit, R., Boyd, M.R. Potent antiinfluenza activity of cyanovirin-N and interactions with viral hemagglutinin. Antimicrob. Agents Chemother. 2003, 47, 2518—2525... 

Another well-studied example is the distribution of the hemagglutinin receptors on the vims surface, which does not allow low-valent systems to efficiently interact with the individual receptors. Therefore, large polyvalent polymeric scaffolds would be ideal candidates to inhibit these biological nano-objects (Fig. 6.25). 

Protein enzyme inhibitors and lectins (hemagglutinins), and their interactions with other molecules, have a broad range of ramifications (Table I). Both classes of proteins are subject to the same set of... 

Influenza A viruses are important human and animal pathogens. Their primary natural hosts are aquatic birds from which they are occasionally transmitted to other species. In man they cause outbreaks of respiratory disease that occur as annual epidemics and less frequent pandemics. Influenza B viruses are also believed to be descendants of avian influenza A viruses, but are now largely restricted to humans where they cause respiratory infections as well. Influenza A and B viruses have two envelope glycoproteins, the hemagglutinin (HA) and the neuraminidase (NA), both of which interact with sialic acid. 

An amphipathic helix is defined as a helix in which the distribution of amino acid residues forms opposing polar and nonpolar faces. It is an important structural unit included in proteins and peptides and is responsible for interaction with biological membranes to elicit their biological functions such as membrane fusion. Influenza virus hemagglutinin [1], fertilin [1], and meltrin-a [2] contain amphipathic fusion peptides, which are likely to adopt a helical conformation during the fusion reaction. To clarify the role of amphipathic peptides in membrane fusion reactions, we synthesized five types of amphipathic model peptides and examined their helix formation, membrane binding and membrane fusion activities. 

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