Structural basis of respiratory syncytial virus neutralization by motavizumab

被引：137

作者：

McLellan, Jason S. ^{[1
]}

Chen, Man ^{[1
]}

Kim, Albert ^{[1
]}

Yang, Yongping ^{[1
]}

Graham, Barney S. ^{[1
]}

Kwong, Peter D. ^{[1
]}

机构：

[1] NIAID, Vaccine Res Ctr, NIH, Bethesda, MD 20892 USA

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2010年 / 17卷 / 02期

关键词：

MONOCLONAL-ANTIBODY; FUSION GLYCOPROTEIN; INFECTION; PROTEIN; PALIVIZUMAB; EPITOPES; INFANTS; BINDING;

D O I：

10.1038/nsmb.1723

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Motavizumab is similar to tenfold more potent than its predecessor, palivizumab (Synagis), the FDA-approved monoclonal antibody used to prevent respiratory syncytial virus (RSV) infection. The structure of motavizumab in complex with a 24-residue peptide corresponding to its epitope on the RSV fusion (F) glycoprotein reveals the structural basis for this greater potency. Modeling suggests that motavizumab recognizes a different quaternary configuration of the F glycoprotein than that observed in a homologous structure.

引用

页码：248 / 250

页数：3

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