Melero, Jose AntonioMas-Lloret, VicenteMcLellan, Jason S2019-11-082019-11-082017Vaccine. 2017 Jan 11;35(3):461-468. doi: 10.1016/j.vaccine.2016.09.045. Epub 2016 Sep 28.0264-410Xhttp://hdl.handle.net/20.500.12105/8566Extraordinary 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.engAMhttp://creativecommons.org/licenses/by-nc-nd/4.0/RSV glycoproteins and vaccine developmentAntigens, ViralGlycoproteinsHumansProtein ConformationRespiratory Syncytial Virus VaccinesRespiratory Syncytial Virus, HumanVirus InternalizationAttribution-NonCommercial-NoDerivatives 4.0 Internacional27692522353461-46810.1016/j.vaccine.2016.09.0451873-2518Vaccineopen access