is an NIH Special Interest Group (SIG)
that organizes seminars and workshops in relevant areas of proteomics,
including talks on separation and protein identification methods,
determination of post-translational modifications, protein-protein
interactions, and bioinformatics and data management. A monthly seminar
series is usually held at 9:30am
on the first Thursday of each month (always check the Mtgs/Seminars
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|April ProtIG Seminar|
|April 6th, 2017|
|9:30am - 10:30am|
|Building 50, NIH Campus|
|John F. Cipollo, Ph.D.|
Vaccine Structure Group, Laboratory of Bacterial Polysaccharides
Center for Biologics Evaluation and Research, Division of Bacterial, Parasitic and Allergenic Products
Food and Drug Administration
|"Characterization of Influenza Hemagglutinin Glycoprotein Antigens: Implications for host – pathogen Interactions and vaccine production."|
Influenza hemagglutinin glycoprotein is the major antigen in seasonal and pandemic influenza vaccines. As the virus propagates through the human population it tends to gain glycosylation sites as part of its adaptive process. This is especially the case for H1N1 and H3N2 influenza strains, two of the three virus subclasses present in the seasonal vaccine. Depending on the virus the surface can have as few as four and as many as 14 glycosylation sites and these tend to be in regions of defined antigenicity implying an antigenic “masking” component of this adaptive process. Some regions may differentially interact with the host’s innate immune system depending on the subclass of glycans present. In the context of vaccines, a number of cell substrates are now used to propagate virus for vaccine production. These include hen egg, MDCK, Vero and Sf9 cell systems with others currently in development. All of these systems will produce cell specific glycosylation patterns, which may impact vaccine performance by influencing antigen uptake, antibody production, innate immune interactions and interaction with components of the host cellular immune system. In this lecture glycomics analytics used in influenza antigen characterization will be discussed. Three cases will be presented revealing aspects of hemagglutinin glycosylation that impact vaccines and influenza’s interactions with the human host. Also discussed will be the application of glycan arrays to influenza study. Hemagglutinin recognizes sialyl glycans on host respiratory tissue in a strain specific fashion. While influenza hemagglutinins binding specificities have been studied extensively using synthetic glycan arrays, how well the glycans on these arrays represent those of host respiratory tissues is currently an area of debate. Strategies to address this issue will be discussed.
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