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00925njm 22002777a 4500 dc Melero, Jose Antonio author Mas-Lloret, Vicente author McLellan, Jason S author 2017 Extraordinary progress in the structure and immunobiology of the human respiratory syncytial virus glycoproteins has been accomplished during the last few years. Determination of the fusion (F) glycoprotein structure folded in either the prefusion or the postfusion conformation was an inspiring breakthrough not only to understand the structural changes associated with the membrane fusion process but additionally to appreciate the antigenic intricacies of the F protein. Furthermore, these developments have opened new avenues for structure-based designs of promising hRSV vaccine candidates. Finally, recent advances in our knowledge of the attachment (G) glycoprotein and its interaction with cell-surface receptors have revitalized interest in this molecule as a vaccine, as well as its role in hRSV immunobiology. Vaccine. 2017 Jan 11;35(3):461-468. doi: 10.1016/j.vaccine.2016.09.045. Epub 2016 Sep 28. 10.1016/j.vaccine.2016.09.045 1873-2518 0264-410X Vaccine 27692522 http://hdl.handle.net/20.500.12105/8566 RSV glycoproteins and vaccine development Structural, antigenic and immunogenic features of respiratory syncytial virus glycoproteins relevant for vaccine development