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Instruments / Technical Area	Publication Details	Published	Actions
I02-Macromolecular Crystallography I04-Macromolecular Crystallography	Recent evolution of equine influenza and the origin of canine influenza Patrick Collins , Sebastien Vachieri , Lesley F. Haire , Roksana Ogrodowicz , Stephen R. Martin , Phil Walker , Xiaoli Xiong , Steven Gamblin , John J. Skehel Proceedings Of The National Academy Of Sciences 111 (30), 11175 - 11180 DOI: 10.1073/pnas.1406606111 PMID: 25024224 Diamond Proposal Number(s): [7707] Show Abstract ▼ Abstract: In 2004 an hemagglutinin 3 neuraminidase 8 (H3N8) equine influenza virus was transmitted from horses to dogs in Florida and subsequently spread throughout the United States and to Europe. To understand the molecular basis of changes in the antigenicity of H3 hemagglutinins (HAs) that have occurred during virus evolution in horses, and to investigate the role of HA in the equine to canine cross-species transfer, we used X-ray crystallography to determine the structures of the HAs from two antigenically distinct equine viruses and from a canine virus. Structurally all three are very similar with the majority of amino acid sequence differences between the two equine HAs located on the virus membrane-distal molecular surface. HAs of canine viruses are distinct in containing a Trp-222→Leu substitution in the receptor binding site that influences specificity for receptor analogs. In the fusion subdomain of canine and recent equine virus HAs a unique difference is observed by comparison with all other HAs examined to date. Analyses of site-specific mutant HAs indicate that a single amino acid substitution, Thr-30→Ser, influences interactions between N-terminal and C-terminal regions of the subdomain that are important in the structural changes required for membrane fusion activity. Both structural modifications may have facilitated the transmission of H3N8 influenza from horses to dogs.	Jul 2014
I03-Macromolecular Crystallography	A Neutralizing Antibody Selected from Plasma Cells That Binds to Group 1 and Group 2 Influenza A Hemagglutinins D. Corti , J. Voss , S. J. Gamblin , G. Codoni , A. Macagno , D. Jarrossay , S. G. Vachieri , D. Pinna , A. Minola , F. Vanzetta , C. Silacci , B. M. Fernandez-rodriguez , G. Agatic , S. Bianchi , I. Giacchetto-sasselli , L. Calder , F. Sallusto , Patrick Collins , L. F. Haire , N. Temperton , J. P. M. Langedijk , John J. Skehel , A. Lanzavecchia Science 333, 850 - 856 DOI: 10.1126/science.1205669 PMID: 21798894 Diamond Proposal Number(s): [1228] Show Abstract ▼ Abstract: The isolation of broadly neutralizing antibodies against influenza A viruses has been a long-sought goal for therapeutic approaches and vaccine design. Using a single-cell culture method for screening large numbers of human plasma cells, we isolated a neutralizing monoclonal antibody that recognized the hemagglutinin (HA) glycoprotein of all 16 subtypes and neutralized both group 1 and group 2 influenza A viruses. Passive transfer of this antibody conferred protection to mice and ferrets. Complexes with HAs from the group 1 H1 and the group 2 H3 subtypes analyzed by x-ray crystallography showed that the antibody bound to a conserved epitope in the F subdomain. This antibody may be used for passive protection and to inform vaccine design because of its broad specificity and neutralization potency.	Aug 2011

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