2026-04-29T20:47:18Zhttps://repisalud.isciii.es/rest/oai/requestoai:repisalud.isciii.es:20.500.12105/85662024-09-27T20:10:30Zcom_20.500.12105_2052com_20.500.12105_2051col_20.500.12105_19609
Repisalud
author
Melero, Jose Antonio
author
Mas-Lloret, Vicente
author
McLellan, Jason S
2019-11-08T11:55:02Z
2019-11-08T11:55:02Z
2017
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
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.
eng
RSV glycoproteins and vaccine development
Structural, antigenic and immunogenic features of respiratory syncytial virus glycoproteins relevant for vaccine development
journal article
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StructuralAntigenicAndImmunogenic_2016.pdf
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StructuralAntigenicAndImmunogenic_2016.pdf.txt