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By Colin W. Ward (auth.), W. Henle, P. H. Hofschneider, H. Koprowski, O. Maaløe, F. Melchers, R. Rott, H. G. Schweiger, P. K. Vogt (eds.)

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200 11) polycrystalline pentagonal dodecahedra, from 65% saturated ammo- Structure of the Influenza Virus Hemagglutinin 29 nium sulphate. Large single octahedral crystals (up to 1 mm3) suitable for X-ray diffraction studies were finally obtained with X-31 BHA when grown from 80% saturated sodium citrate (Wil~ and SkeheI1977). 1981). The structure was determined using a single isomorphous derivative, mercury phenylglyoxal, and 11 cycles of noncrystallographic threefold symmetry averaging. 4 A. Initially it was believed that the asymmetric unit contained two BHA trimers (Wil~ and SkeheI1977), but the final electron density maps clearly indicated one hemagglutinin trimer per asymmetric unit (Wilson et al.

Ward Fig. 5. Stereo drawing of the alpha carbon tracing of an influenza hemagglutinin monomer (HAl and HA2) with a schematic diagram on the right showing ~-sheetstrands (flat twisted arrows), a-helices (cylinders), and disulphide bonds (filled circles). The hexose ring positions are tentatively shown in the stereo drawing as open circles. Insert: Shows the eight-stranded ~-sheet structure and looped out regions in the globular domain. Data is from Wilson et aI. (1981) Structure of the Influenza Virus Hemagglutinin 31 There are two looped-out regions between strands in the j3-structure: the 125-163 loop between p-strands 1and 2 and the 187-199 a-helix containing loop between j3-strands 3 and 4.

2 Studies with Fractionated Antisera Adsorption experiments (Laver et al. 1974; Virelezier et al. 1974) showed that when antiHA sera were adsorbed with a related strain of virus, the antibody molecules removed by adsorption could react with both virus strains and were designated "common" or crossreacting antibodies while the IgG molecules left behind in the supernatant could only react with the virus used as immunogen and were designated "specific" to that virus. These observations have been widely confIrmed and generally interpreted in terms of topographically distinct common and specific antigenic determinants (Laver et al.

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