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Document 18 The Design of Anti-Influenza Virus Drugs from the X-ray Molecular Structure of Influenza Virus Neuraminidase Joseph N. Varghese Biomolecular Research Institute, Melbourne, Victoria, Australia I. Introduction Page 459 Influenza has plagued humankind since the dawn of history and continues to affect a significant proportion of the population irrespective of age or previous infection history. These periodic epidemics that reinfect otherwise healthy people have devastated communities world wide. Some pandemics like the 1917–1919 “Spanish flu” were responsible for the death of tens of millions of people throughout the world. The origins, spread, and severity of influenza epidemics have been a puzzle that has only in the last two decades been adequately addressed. In early times it was thought that the disease was the evil influence (sic) of the stars, and other extraterrestial objects. At present it is generally accepted that the disease is of viral origin, spread by aerosols produced by infected animals, and the continual production of new strains of the virus results in reinfection of the disease (reviewed in Reference 1). There are three types of influenza virus classified on their serological cross-reactivity with viral matrix proteins and soluble nucleoprotein (A, B, and C). Only type A and B are known to cause severe human disease. Type B is only found in humans, while type A has a natural reservoir in birds and some mammals like pigs and horses [2]. Influenza, an orthomyxovirus, is a 100 nm lipid-enveloped virus (Figure 1) containing an eight-segment negative single-stranded genome [3]. Two of the segments code for the surfaces glycoproteins, hemagglutinin (which binds to terminal sialic acid), and neuraminidase (which http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_459.html [4/9/2004 12:12:33 AM]
Document Figure 1 A schematic diagram of an influenza virus particle that illustrates its constituent components and morphology. The surface antigens hemagglutinin and neuraminidase are attached to the lipid and matrix protein shell that encapsulates the eight negative-stranded RNA genes of the virus and associated nucleoprotein and polymerase. Page 460 cleaves terminal sialic acid) and which appear as spikes protruding out of the viral envelope. The viral target in humans is the upper respiratory tract epithelial cells. Replication (see Figure 2) begins with penetration of the virion through the mucin layer covering the epithelial surface, followed by attachment to the viral receptor by the hemagglutinin. Penetration of the cell is achieved by endocytosis and the virion core is released after the fusion of the virion and vesicle membrane mediated by the hemagglutinin. Fusion is enabled by a conformational change in the hemagglutinin made possible by lowering the pH of the endosome by the M2 ion channel protein. Following replication, the progeny virions are released by budding off the cell membrane [4,5]. http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_460.html (1 of 2) [4/9/2004 12:12:42 AM]
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