Discrete conformations of epitope II on the hepatitis C virus E2 protein for antibody-mediated neutralization and nonneutralization

作者：Deng Lu; Ma Li; Virata Theimer Maria Luisa; Zhong Lilin; Yan Hailing; Zhao Zhong; Struble Evi; Feinstone Stephen; Alter Harvey^*; Zhang Pei

来源：Proceedings of the National Academy of Sciences of the United States of America, 2014, 111(29): 10690-10695.

DOI：10.1073/pnas.1411317111

• immunoglobulins
• prophylaxis
• vaccine

The X-ray crystal structure of epitope II on the E2 protein of hepatitis C virus, in complex with nonneutralizing antibody mAb#12, has been solved at 2.90-angstrom resolution. The spatial arrangement of the essential components of epitope II (ie, the C-terminal a-helix and the N-terminal loop) was found to deviate significantly from that observed in those corresponding complexes with neutralizing antibodies. The distinct conformations are mediated largely by the flexibility of a highly conserved glycine residue that connects these components. Thus, it is the particular tertiary structure of epitope II, which is presented in a spatial and temporal manner, that determines the specificity of antibody recognition and, consequently, the outcome of neutralization or nonneutralization.

• 出版日期2014-7-22
• 单位NIH