Hemagglutinin Receptor Binding Avidity Drives Influenza A Virus Antigenic Drift Export

@article{citeulike:6100419, abstract = {Rapid antigenic evolution in the influenza A virus hemagglutinin precludes effective vaccination with existing vaccines. To understand this phenomenon, we passaged virus in mice immunized with influenza vaccine. Neutralizing antibodies selected mutants with single-amino acid hemagglutinin substitutions that increased virus binding to cell surface glycan receptors. Passaging these high-avidity binding mutants in naive mice, but not immune mice, selected for additional hemagglutinin substitutions that decreased cellular receptor binding avidity. Analyzing a panel of monoclonal antibody hemagglutinin escape mutants revealed a positive correlation between receptor binding avidity and escape from polyclonal antibodies. We propose that in response to variation in neutralizing antibody pressure between individuals, influenza A virus evolves by adjusting receptor binding avidity via amino acid substitutions throughout the hemagglutinin globular domain, many of which simultaneously alter antigenicity. 10.1126/science.1178258}, author = {Hensley, Scott E. and Das, Suman R. and Bailey, Adam L. and Schmidt, Loren M. and Hickman, Heather D. and Jayaraman, Akila and Viswanathan, Karthik and Raman, Rahul and Sasisekharan, Ram and Bennink, Jack R. and Yewdell, Jonathan W.}, citeulike-article-id = {6100419}, citeulike-linkout-0 = {http://dx.doi.org/10.1126/science.1178258}, citeulike-linkout-1 = {http://www.sciencemag.org/content/326/5953/734.abstract}, citeulike-linkout-2 = {http://www.sciencemag.org/content/326/5953/734.full.pdf}, citeulike-linkout-3 = {http://view.ncbi.nlm.nih.gov/pubmed/19900932}, citeulike-linkout-4 = {http://www.hubmed.org/display.cgi?uids=19900932}, day = {30}, doi = {10.1126/science.1178258}, journal = {Science}, keywords = {antigen, influenza}, month = {October}, number = {5953}, pages = {734--736}, posted-at = {2009-11-12 02:51:48}, priority = {2}, title = {Hemagglutinin Receptor Binding Avidity Drives Influenza A Virus Antigenic Drift}, url = {http://dx.doi.org/10.1126/science.1178258}, volume = {326}, year = {2009} }

TY - JOUR ID - citeulike:6100419 L3 - citeulike-article-id:6100419 N2 - Rapid antigenic evolution in the influenza A virus hemagglutinin precludes effective vaccination with existing vaccines. To understand this phenomenon, we passaged virus in mice immunized with influenza vaccine. Neutralizing antibodies selected mutants with single-amino acid hemagglutinin substitutions that increased virus binding to cell surface glycan receptors. Passaging these high-avidity binding mutants in naive mice, but not immune mice, selected for additional hemagglutinin substitutions that decreased cellular receptor binding avidity. Analyzing a panel of monoclonal antibody hemagglutinin escape mutants revealed a positive correlation between receptor binding avidity and escape from polyclonal antibodies. We propose that in response to variation in neutralizing antibody pressure between individuals, influenza A virus evolves by adjusting receptor binding avidity via amino acid substitutions throughout the hemagglutinin globular domain, many of which simultaneously alter antigenicity. 10.1126/science.1178258 IS - 5953 JF - Science EP - 736 TI - Hemagglutinin Receptor Binding Avidity Drives Influenza A Virus Antigenic Drift VL - 326 SP - 734 KW - antigen KW - influenza AU - Hensley, Scott AU - Das, Suman AU - Bailey, Adam AU - Schmidt, Loren AU - Hickman, Heather AU - Jayaraman, Akila AU - Viswanathan, Karthik AU - Raman, Rahul AU - Sasisekharan, Ram AU - Bennink, Jack AU - Yewdell, Jonathan PY - 2009/10/30/ UR - http://dx.doi.org/10.1126/science.1178258 ER -