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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...

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Autores principales: Deng, Lu, Ma, Li, Virata, Maria Luisa, Zhong, Lilin, Yan, Hailing, Zhao, Zhong, Struble, Evi, Feinstone, Stephen, Alter, Harvey, Zhang, Pei
Formato: Online Artículo Texto
Lenguaje:English
Publicado: National Academy of Sciences 2014
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.
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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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