Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 111, Issue 29, Pages 10690-10695Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1411317111
Keywords
immunoglobulins; prophylaxis; vaccine
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Funding
- US Department of Energy Offices of Biological and Environmental Research and Basic Energy Sciences
- National Center for Research Resources of the National Institutes of Health
- CBER
- FDA
- Research Participation Program at CBER
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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.
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