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TitleMutating a flexible region of the RSV F protein can stabilize the prefusion conformation.
Journal, issue, pagesScience, Vol. 385, Issue 6716, Page 1484-1491, Year 2024
Publish dateSep 27, 2024
AuthorsYu Liang / Shuai Shao / Xin Yu Li / Zi Xin Zhao / Ning Liu / Zhao Ming Liu / Fu Jie Shen / Hao Zhang / Jun Wei Hou / Xue Feng Zhang / Yu Qin Jin / Li Fang Du / Xin Li / Jing Zhang / Ji Guo Su / Qi Ming Li /
PubMed AbstractThe respiratory syncytial virus (RSV) fusion (F) glycoprotein is highly immunogenic in its prefusion (pre-F) conformation. However, the protein is unstable, and its conformation must be stabilized ...The respiratory syncytial virus (RSV) fusion (F) glycoprotein is highly immunogenic in its prefusion (pre-F) conformation. However, the protein is unstable, and its conformation must be stabilized for it to function effectively as an immunogen in vaccines. We present a mutagenesis strategy to arrest the RSV F protein in its pre-F state by blocking localized changes in protein structure that accompany large-scale conformational rearrangements. We generated a series of mutants and screened them in vitro to assess their potential for forming a stable pre-F. In animals, the immunogenicity of a representative mutant F protein, with a conformation confirmed by cryo-electron microscopy, elicited levels of neutralizing antibodies and protection against RSV-induced lung damage that were comparable to those of DS-Cav1, a pre-F used in a licensed vaccine.
External linksScience / PubMed:39325881
MethodsEM (single particle)
Resolution3.4 Å
Structure data

39188

8ye3

EMDB-39188, PDB-8ye3:
Cryo-EM structure of human respiratory syncytial virus fusion protein variant
Method: EM (single particle) / Resolution: 3.4 Å

Source
  • human respiratory syncytial virus
KeywordsVIRAL PROTEIN / RSV / Fusion Glycoprotein / Pre-fusion

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