Author: Boyington, Jeffrey C.; Joyce, M. Gordon; Sastry, Mallika; Stewart-Jones, Guillaume B. E.; Chen, Man; Kong, Wing-Pui; Ngwuta, Joan O.; Thomas, Paul V.; Tsybovsky, Yaroslav; Yang, Yongping; Zhang, Baoshan; Chen, Lei; Druz, Aliaksandr; Georgiev, Ivelin S.; Ko, Kiyoon; Zhou, Tongqing; Mascola, John R.; Graham, Barney S.; Kwong, Peter D.
Title: Structure-Based Design of Head-Only Fusion Glycoprotein Immunogens for Respiratory Syncytial Virus Document date: 2016_7_27
ID: 1nbocmux_1
Snippet: Human respiratory syncytial virus (RSV) infects most children by the age of two, with re-infection occurring sporadically throughout life [1] . Young children and the elderly are especially at risk of severe lower respiratory tract infection resulting in extensive morbidity and over 3.4 million hospitalizations per year [2] [3] [4] . The development of an RSV vaccine is thus a priority. To date, the most potently RSV-neutralizing antibodies recog.....
Document: Human respiratory syncytial virus (RSV) infects most children by the age of two, with re-infection occurring sporadically throughout life [1] . Young children and the elderly are especially at risk of severe lower respiratory tract infection resulting in extensive morbidity and over 3.4 million hospitalizations per year [2] [3] [4] . The development of an RSV vaccine is thus a priority. To date, the most potently RSV-neutralizing antibodies recognize the RSV fusion (F) surface glycoprotein [5] . RSV F is a type I fusion glycoprotein, comprising an F 0 precursor which is activated by furin cleavage to form a prefusion (pre-F) trimer of disulfide-linked F 2 and F 1 heterodimers [6] . The pre-F conformation of RSV F undergoes substantial structural rearrangements as it transitions to the post-fusion conformation, as part of its essential role in merging viral and host cell membranes during entry.
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