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Basic Characteristics of Mutations
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Mutation Site
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N448Q |
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Mutation Site Sentence
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While the presence of glycan N4 thus potentially complicates the design of an efficient E2 vaccine targeting the hydrophobic protrusion within epitope II, the viability of a mutant N448Q HCVcc JFH-1 virus is not compromised, indicating a valid alternative for both life vaccines and subunit vaccines consisting of recombinant HCV E2. |
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Mutation Level
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Amino acid level |
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Mutation Type
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Nonsynonymous substitution |
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Gene/Protein/Region
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E2 |
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Standardized Encoding Gene
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E2
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Genotype/Subtype
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- |
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Viral Reference
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-
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Functional Impact and Mechanisms
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Disease
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HCV Infection
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Immune
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- |
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Target Gene
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-
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Clinical and Epidemiological Correlations
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Clinical Information
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- |
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Treatment
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- |
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Location
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- |
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Literature Information
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PMID
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23696737
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Title
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Structural basis of HCV neutralization by human monoclonal antibodies resistant to viral neutralization escape
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Author
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Krey T,Meola A,Keck ZY,Damier-Piolle L,Foung SK,Rey FA
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Journal
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PLoS pathogens
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Journal Info
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2013;9(5):e1003364
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Abstract
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The high mutation rate of hepatitis C virus allows it to rapidly evade the humoral immune response. However, certain epitopes in the envelope glycoproteins cannot vary without compromising virus viability. Antibodies targeting these epitopes are resistant to viral escape from neutralization and understanding their binding-mode is important for vaccine design. Human monoclonal antibodies HC84-1 and HC84-27 target conformational epitopes overlapping the CD81 receptor-binding site, formed by segments aa434-446 and aa610-619 within the major HCV glycoprotein E2. No neutralization escape was yet observed for these antibodies. We report here the crystal structures of their Fab fragments in complex with a synthetic peptide comprising aa434-446. The structures show that the peptide adopts an alpha-helical conformation with the main contact residues F(4)(4)(2) and Y(4)(4)(3) forming a hydrophobic protrusion. The peptide retained its conformation in both complexes, independently of crystal packing, indicating that it reflects a surface feature of the folded glycoprotein that is exposed similarly on the virion. The same residues of E2 are also involved in interaction with CD81, suggesting that the cellular receptor binds the same surface feature and potential escape mutants critically compromise receptor binding. In summary, our results identify a critical structural motif at the E2 surface, which is essential for virus propagation and therefore represents an ideal candidate for structure-based immunogen design for vaccine development.
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Sequence Data
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-
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