Structural basis of influenza virus neutralization
- 11 January 2011
- journal article
- review article
- Published by Wiley in Annals of the New York Academy of Sciences
- Vol. 1217 (1) , 178-190
- https://doi.org/10.1111/j.1749-6632.2010.05829.x
Abstract
Although seasonal influenza vaccines play a valuable role in reducing the spread of virus at the population level, ongoing viral evolution to evade immune responses remains problematic. No current vaccines elicit enduring protection in the face of emerging and re‐emerging influenza viruses that are rapidly undergoing antigenic drift. Eliciting broadly cross‐neutralizing antibody (nAb) responses against influenza virus is a crucial goal for seasonal and pandemic influenza vaccine preparation. Recent three‐dimensional structure information obtained from crystallization of influenza antigens in complex with nAbs has provided a framework for interpreting antibody‐based viral neutralization that should aid in the design of vaccine immunogens. Here, we will review current knowledge of the structure‐based mechanisms contributing to the neutralization and neutralization escape of influenza viruses. We will also explore the potential for this structure‐based approach to overcome the obstacles in developing the highly desired “universal” influenza vaccine.Keywords
This publication has 92 references indexed in Scilit:
- Epidermal injury and infection during poxvirus immunization is crucial for the generation of highly protective T cell–mediated immunityNature Medicine, 2010
- Structural and functional bases for broad-spectrum neutralization of avian and human influenza A virusesNature Structural & Molecular Biology, 2009
- Detecting influenza epidemics using search engine query dataNature, 2009
- Analysis of residues near the fusion peptide in the influenza hemagglutinin structure for roles in triggering membrane fusionVirology, 2007
- Haemagglutinin mutations responsible for the binding of H5N1 influenza A viruses to human-type receptorsNature, 2006
- UCSF Chimera—A visualization system for exploratory research and analysisJournal of Computational Chemistry, 2004
- H1 and H7 influenza haemagglutinin structures extend a structural classification of haemagglutinin subtypesVirology, 2004
- Structure of influenza haemagglutinin at the pH of membrane fusionNature, 1994
- A spring-loaded mechanism for the conformational change of influenza hemagglutininCell, 1993
- Introduction of intersubunit disulfide bonds in the membrane-distal region of the influenza hemagglutinin abolishes membrane fusion activityCell, 1992