Structural studies on antibody recognition and neutralization of viruses

The purpose of this brief review is to highlight how structural information can elucidate antibody recognition and neutralization of viruses. Studies on human rhinovirus demonstrated that antibodies need not induce conformational changes for neutralization and that viruses do not conceal receptor-binding regions from immune recognition. Ross River and Sindbis virus complexes were an early example of using antibodies to demark receptor-binding regions. The structure of an antibody bound to mouse norovirus is an example of antibodies binding to sharp protrusions on flexible receptor-binding domains. Finally, the structure of cucumber mosaic virus bound to a loop involved in aphid transmission demonstrated the importance of the context of antigen presentation and what happens when an antibody binds near an icosahedral symmetry axis.

► Antibodies do not cause conformational changes in viral capsids upon neutralization. ► Receptor binding regions are not hidden from antibody recognition. ► It may be possible to target vaccines to conserved portions of viruses that are dynamically exposed during capsid breathing.