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Structure basis of neutralization by a novel site II/IV antibody against respiratory syncytial virus fusion protein.
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- المؤلفون: Xie, Qingqing1,2; Wang, Zhao2; Ni, Fengyun2; Chen, Xiaorui2; Ma, Jianpeng1,2; Patel, Nita3; Lu, Hanxin3; Liu, Ye3; Tian, Jing-Hui3; Flyer, David3; Massare, Michael J.3; Ellingsworth, Larry3; Glenn, Gregory3; Smith, Gale3 ; Wang, Qinghua2
- المصدر:
PLoS ONE. 2/7/2019, Vol. 14 Issue 2, p1-20. 20p.
- الموضوع:
- معلومة اضافية
- نبذة مختصرة :
Globally, human respiratory syncytial virus (RSV) is a leading cause of lower respiratory tract infections in newborns, young children, and the elderly for which there is no vaccine. The RSV fusion (F) glycoprotein is a major target for vaccine development. Here, we describe a novel monoclonal antibody (designated as R4.C6) that recognizes both pre-fusion and post-fusion RSV F, and binds with nanomole affinity to a unique neutralizing site comprised of antigenic sites II and IV on the globular head. A 3.9 Å-resolution structure of RSV F-R4.C6 Fab complex was obtained by single particle cryo-electron microscopy and 3D reconstruction. The structure unraveled detailed interactions of R4.C6 with antigenic site II on one protomer and site IV on a neighboring protomer of post-fusion RSV F protein. These findings significantly further our understanding of the antigenic complexity of the F protein and provide new insights into RSV vaccine design. [ABSTRACT FROM AUTHOR]
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