Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation
DC Wiley, IA Wilson, JJ Skehel - Nature, 1981 - nature.com
DC Wiley, IA Wilson, JJ Skehel
Nature, 1981•nature.coma rather specific role for the terminal sequence in the fusion Page 1 Nature Vol. 289 29 January
1981 373 (100% in signals, 85% in hydrophobic tails), which suggests a rather specific role for
the terminal sequence in the fusion process. There are two obvious difficulties in understanding
the role of haemagglutinins in membrane fusion. First, the 135 Ålength of the haemagglutinin
seems to restrict membranes from any closer initial approach. Second, the HA, amino-terminus
is -100 Å from the distal tip and 35 Å from the membrane end of the molecule. For this region …
1981 373 (100% in signals, 85% in hydrophobic tails), which suggests a rather specific role for
the terminal sequence in the fusion process. There are two obvious difficulties in understanding
the role of haemagglutinins in membrane fusion. First, the 135 Ålength of the haemagglutinin
seems to restrict membranes from any closer initial approach. Second, the HA, amino-terminus
is -100 Å from the distal tip and 35 Å from the membrane end of the molecule. For this region …
Abstract
Four ‘antigenic sites’ on the three-dimensional structure of the influenza haemagglutinin are identified. At least one amino acid substitution in each site seems to be required for the production of new epidemic strains between 1968 and 1975.
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