The overall goal of our work is to find effective ways of controlling influenza in the human population. Influenza viruses have enormous capacity for variation, thus they can rapidly mutate and escape from the antibodies raised in response to infection or vaccination.
Influenza viruses can similarly mutate to escape from inhibition by anti-influenza drugs.
We are following two main lines of research. The first is aimed at finding ways to make better vaccines by understanding the structural level how the virus escapes from antibodies. We are using antibody selection and directed mutagenesis of the viral surface antigens to determine the precise mechanism of virus escape from monoclonal antibodies and hence from the host immune system. Influenza neuraminidase was the first example of a crystal structure of viral antigen complexed with antibody, thus we have a uniquely defined system under study. We have determined for the epitope recognized by antibody NC41 that, although 19 amino acids of the neuraminidase are in contact with antibody, only three of these are essential to the interaction.