About: Junctional and somatic hypermutation-induced CX(4)C motif is critical for the recognition of a highly conserved epitope on HCV E2 by a human broadly neutralizing antibody

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Junctional and somatic hypermutation-induced CX(4)C motif is critical for the recognition of a highly conserved epitope on HCV E2 by a human broadly neutralizing antibody Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Junctional and somatic hypermutation-induced CX(4)C motif is critical for the recognition of a highly conserved epitope on HCV E2 by a human broadly neutralizing antibody
Creator	Yan, Yu Ye, Sheng Zhang, Rongguang Sun, Bing Niu, Junqi Huang, Zhong Xia, Jing Sun, Xiaoyu Zhang, Ronghua Zhong, Jin Wang, Xuesong Ling, Zhiyang Yi, Chunyan Zhang, Yaguang Ma, Liyan Fan, Weiguo He, Lan Long, Gang Lu, Junxia Wang, Jiangjun Xu, Yongfen Zhao, Xinhao Zhou, Honglin
Source	PMC
abstract	Induction of broadly neutralizing monoclonal antibodies (bNAbs) that bind to the viral envelope glycoproteins is a major goal of hepatitis C virus (HCV) vaccine research. The study of bNAbs arising in natural infection is essential in this endeavor. We generated a human antibody, 8D6, recognizing the E2 protein of HCV isolated from a chronic hepatitis C patient. This antibody shows broadly neutralizing activity, which covers a pan-genotypic panel of cell culture-derived HCV virions (HCVcc). Functional and epitope analyses demonstrated that 8D6 can block the interaction between E2 and CD81 by targeting a highly conserved epitope on E2. We describe how the 8D6 lineage evolved via somatic hypermutation to achieve broad neutralization. We found that the V(D)J recombination-generated junctional and somatic hypermutation-induced disulfide bridge (C-C) motif in the CDRH3 is critical for the broad neutralization and binding activity of 8D6. This motif is conserved among a series of broadly neutralizing HCV antibodies, indicating a common binding model. Next, the 8D6 inferred germline (iGL) was reconstructed and tested for its binding affinity and neutralization activity. Interestingly, 8D6 iGL-mediated relatively strong inhibition of the 1b genotype PR79L9 strain, suggesting that PR79L9 may serve as a potential natural viral strain that provides E2 sequences that induce bNAbs. Overall, our detailed epitope mapping and genetic studies of the HCV E2-specific mAb 8D6 have allowed for further refinement of antigenic sites on E2 and reveal a new mechanism to generate a functional CDRH3, while its iGL can serve as a probe to identify potential HCV vaccine strains.
has issue date	2020-03-31(xsd:dateTime)
bibo:doi	10.1038/s41423-020-0403-1
bibo:pmid	32235917
has license	no-cc
sha1sum (hex)	d88f5e74983640e30e8b5818cc0e2e2a9d3fb692
schema:url	https://doi.org/10.1038/s41423-020-0403-1
resource representing a document's title	Junctional and somatic hypermutation-induced CX(4)C motif is critical for the recognition of a highly conserved epitope on HCV E2 by a human broadly neutralizing antibody
has PubMed Central identifier	PMC7222171
has PubMed identifier	32235917
schema:publication	Cell Mol Immunol
resource representing a document's body	covid:d88f5e74983640e30e8b5818cc0e2e2a9d3fb692#body_text
is schema:about of	named entity 'HCV' named entity 'This' named entity 'genetic studies' named entity 'strains' named entity 'infection' named entity 'neutralizing' named entity 'conserved' named entity 'epitope' named entity 'broad' named entity 'mechanism' named entity 'bind' named entity 'neutralizing' named entity 'model' named entity 'chronic hepatitis C' named entity 'antibodies' named entity 'Induction' named entity 'broadly' named entity 'Next' named entity 'neutralization' named entity 'analyses' named entity 'sequences' named entity 'demonstrated' named entity 'evolved' named entity 'vaccine' named entity 'C-C' named entity 'genetic studies' named entity 'somatic hypermutation' named entity 'highly conserved' named entity 'antibody' named entity 'motif' named entity 'motif' named entity 'vaccine' named entity 'viral envelope' named entity 'somatic hypermutation' named entity 'hepatitis C virus' named entity 'monoclonal antibodies' named entity 'genotypic' named entity 'cell culture' named entity 'binding activity' named entity 'infection' named entity 'mAb' named entity 'motif' named entity 'broad' named entity 'antibody' named entity 'glycans' named entity 'infection' named entity 'linear epitope' named entity 'serially diluted' named entity 'penicillin' named entity 'antibody engineering' named entity 'Immunofluorescence' named entity 'gene' named entity 'TMB' named entity 'cysteine' named entity 'structural model' named entity 'HCV' named entity 'PDB' named entity 'genotypes' named entity 'antibodies'

Faceted Search & Find service v1.13.91 as of Mar 24 2020

Alternative Linked Data Documents: Sponger | ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3229 as of Jul 10 2020, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (94 GB total memory)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software