Abstract
Evaluation of: Aoki ST, Settembre EC, Trask SD, Greenberg HB, Harrison SC, Dormitzer PR: Structure of rotavirus outer-layer protein VP7 bound with a neutralizing Fab. Science 324 (5993), 1444–1447 (2009). The determination of the molecular structure of the trimer of VP7, one of the outer layer proteins of rotaviruses, has significantly contributed to the knowledge of the overall structure of rotavirus particles. The molecular mechanism of rotavirus neutralization has been clarified and a topological explanation been found for the emergence of antibody escape mutants. Furthermore, translational work was enabled by engineering VP7 mutants, which form stable trimers by means of novel disulfide bridges linking the different subunits together; such a construct could become an attractive and safe vaccine candidate.
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