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Discrete conformations of epitope II on the hepatitis C virus E2 protein for antibody-mediated neutralization and nonneutralization
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-Å resolution. The spatial arrangement of the essential components of epitope II (ie, the C-terminal α-helix and the N-terminal loop) was found to...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
National Academy of Sciences
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4115556/ https://www.ncbi.nlm.nih.gov/pubmed/25002515 http://dx.doi.org/10.1073/pnas.1411317111 |
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author | Deng, Lu Ma, Li Virata, Maria Luisa Zhong, Lilin Yan, Hailing Zhao, Zhong Struble, Evi Feinstone, Stephen Alter, Harvey Zhang, Pei |
author_facet | Deng, Lu Ma, Li Virata, Maria Luisa Zhong, Lilin Yan, Hailing Zhao, Zhong Struble, Evi Feinstone, Stephen Alter, Harvey Zhang, Pei |
author_sort | Deng, Lu |
collection | PubMed |
description | 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-Å resolution. The spatial arrangement of the essential components of epitope II (ie, the C-terminal α-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. |
format | Online Article Text |
id | pubmed-4115556 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | National Academy of Sciences |
record_format | MEDLINE/PubMed |
spelling | pubmed-41155562014-08-05 Discrete conformations of epitope II on the hepatitis C virus E2 protein for antibody-mediated neutralization and nonneutralization Deng, Lu Ma, Li Virata, Maria Luisa Zhong, Lilin Yan, Hailing Zhao, Zhong Struble, Evi Feinstone, Stephen Alter, Harvey Zhang, Pei Proc Natl Acad Sci U S A Biological Sciences 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-Å resolution. The spatial arrangement of the essential components of epitope II (ie, the C-terminal α-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. National Academy of Sciences 2014-07-22 2014-07-07 /pmc/articles/PMC4115556/ /pubmed/25002515 http://dx.doi.org/10.1073/pnas.1411317111 Text en Freely available online through the PNAS open access option. |
spellingShingle | Biological Sciences Deng, Lu Ma, Li Virata, Maria Luisa Zhong, Lilin Yan, Hailing Zhao, Zhong Struble, Evi Feinstone, Stephen Alter, Harvey Zhang, Pei Discrete conformations of epitope II on the hepatitis C virus E2 protein for antibody-mediated neutralization and nonneutralization |
title | Discrete conformations of epitope II on the hepatitis C virus E2 protein for antibody-mediated neutralization and nonneutralization |
title_full | Discrete conformations of epitope II on the hepatitis C virus E2 protein for antibody-mediated neutralization and nonneutralization |
title_fullStr | Discrete conformations of epitope II on the hepatitis C virus E2 protein for antibody-mediated neutralization and nonneutralization |
title_full_unstemmed | Discrete conformations of epitope II on the hepatitis C virus E2 protein for antibody-mediated neutralization and nonneutralization |
title_short | Discrete conformations of epitope II on the hepatitis C virus E2 protein for antibody-mediated neutralization and nonneutralization |
title_sort | discrete conformations of epitope ii on the hepatitis c virus e2 protein for antibody-mediated neutralization and nonneutralization |
topic | Biological Sciences |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4115556/ https://www.ncbi.nlm.nih.gov/pubmed/25002515 http://dx.doi.org/10.1073/pnas.1411317111 |
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