Ian Wilson, The Scripps Research Institute, La Jolla, USA
5th July 2017 at 12:00pm [Download iCalendar / .ics file]
Until relatively recently, most antibodies to influenza virus were thought to be strain-specific and protect only against highly related strains within the same subtype. Since 2008, many human antibodies have been isolated that are much broader and neutralize across different subtypes and types of influenza viruses through binding to functionally conserved sites. The major surface antigen, the hemagglutinin (HA), of influenza virus is the main target of these neutralizing antibodies. We have determined crystal structures of several broadly neutralizing human antibodies in complex with variety of different HAs and show they bind to the highly conserved functional sites on the HA fusion domain (stem) in influenza A as well as influenza B viruses, as well as to the receptor binding site. The characterization of these broadly neutralizing antibodies along with their mode of binding and neutralization has provided exciting new opportunities for structure-assisted vaccine design and for design of therapeutics that afford greater protection against influenza viruses. Indeed, a mini-HA immunogen that was designed to mimic the highly conserved HA stem elicited a protective response against different influenza subtypes, such as H1N1 and H5N1, in mice and monkeys and is a promising proof of concept for development of a more universal flu vaccine. We also recently determined the structure of a broad anti-viral small molecule arbidol and elucidated its binding site and mechanism of action.
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