About: Characterization of a Monoclonal Antibody to a Novel Glycan-Dependent Epitope in the V1/V2 Domain of the HIV-1 Envelope Protein, gp120

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About: Characterization of a Monoclonal Antibody to a Novel Glycan-Dependent Epitope in the V1/V2 Domain of the HIV-1 Envelope Protein, gp120 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	Characterization of a Monoclonal Antibody to a Novel Glycan-Dependent Epitope in the V1/V2 Domain of the HIV-1 Envelope Protein, gp120
Creator	Yu, Bin Berman, Phillip Doran, Rachel Mesa, Kathryn Morales, Javier Morin, Trevor O'rourke, Sara Theolis, Richard To, Briana
Source	Elsevier; Medline; PMC
abstract	Recent studies have described several broadly neutralizing monoclonal antibodies (bN-mAbs) that recognize glycan-dependent epitopes (GDEs) in the HIV-1 envelope protein, gp120. These were recovered from HIV-1 infected subjects, and several (e.g., PG9, PG16, CH01, CH03) target glycans in the first and second variable (V1/V2) domain of gp120. The V1/V2 domain is thought to play an important role in conformational masking, and antibodies to the V1/V2 domain were recently identified as the only immune response that correlated with protection in the RV144 HIV-1 vaccine trial. While the importance of antibodies to polymeric glycans is well established for vaccines targeting bacterial diseases, the importance of antibodies to glycans in vaccines targeting HIV has only recently been recognized. Antibodies to GDEs may be particularly significant in HIV vaccines based on gp120, where 50% of the molecular mass of the envelope protein is contributed by N-linked carbohydrate. However, few studies have reported antibodies to GDEs in humans or animals immunized with candidate HIV-1 vaccines. In this report, we describe the isolation of a mouse mAb, 4B6, after immunization with the extracellular domain of the HIV-1 envelope protein, gp140. Epitope mapping using glycopeptide fragments and in vitro mutagenesis showed that binding of this antibody depends on N-linked glycosylation at asparagine N130 (HXB2 numbering) in the gp120 V1/V2 domain. Our results demonstrate that, in addition to natural HIV-1 infection, immunization with recombinant proteins can elicit antibodies to the GDEs in the V1/V2 domain of gp120. Although little is known regarding conditions that favor antibody responses to GDEs, our studies demonstrate that these antibodies can arise from a short-term immunization regimen. Our results suggest that antibodies to GDEs are more common than previously suspected, and that further analysis of antibody responses to the HIV-1 envelope protein will lead to the discovery of additional antibodies to GDEs.
has issue date	2014-11-01(xsd:dateTime)
bibo:doi	10.1016/j.molimm.2014.06.025
bibo:pmid	25016576
has license	green-oa
sha1sum (hex)	8a5bf2b16d131fbee41247f16dc53c0fd3511c3e
schema:url	https://doi.org/10.1016/j.molimm.2014.06.025
resource representing a document's title	Characterization of a Monoclonal Antibody to a Novel Glycan-Dependent Epitope in the V1/V2 Domain of the HIV-1 Envelope Protein, gp120
has PubMed Central identifier	PMC4157072
has PubMed identifier	25016576
schema:publication	Molecular Immunology
resource representing a document's body	covid:8a5bf2b16d131fbee41247f16dc53c0fd3511c3e#body_text
is schema:about of	named entity 'NOVEL' named entity 'based' named entity 'humans' named entity 'recognize' named entity 'domain' named entity 'HIV-1' named entity 'play' named entity 'GLYCAN' named entity 'ACCESS' named entity 'GP120' named entity 'DEPENDENT' named entity 'EPITOPE' named entity 'MAY BE' named entity 'USING' named entity 'RECOGNIZE' named entity 'IDENTIFIED' named entity 'HIV-1 INFECTION' named entity 'HIV' named entity 'SIGNIFICANT' named entity 'FRAGMENTS' named entity 'DOMAIN' named entity 'MOLECULAR MASS' named entity 'NATURAL' named entity 'ADDITION' named entity 'TARGETING' named entity 'DESCRIBED' named entity 'NIH' named entity 'VACCINES' named entity 'POLYMERIC' named entity 'REGIMEN' named entity 'IMMUNIZATION' named entity 'FAVOR' named entity 'ANIMALS' named entity 'TARGET' named entity 'ADDITIONAL' named entity 'EPITOPES' named entity 'HAVE' named entity 'RESPONSES' named entity 'INFECTED' named entity 'A MOUSE' named entity 'ISOLATION' named entity 'CARBOHYDRATE' named entity 'ANTIBODY' named entity 'MONOCLONAL ANTIBODIES' named entity 'BINDING' named entity 'AUTHOR' named entity 'MAB' named entity 'COMMON' named entity 'RECENT' named entity 'IMMUNIZED' named entity 'SECOND' named entity 'ANTIBODIES' named entity 'PLAY' named entity 'LEAD' named entity 'HIV-1' named entity 'PUBLIC' named entity 'DOMAIN' named entity 'ENVELOPE PROTEIN' named entity 'MASKING' named entity 'ESTABLISHED' named entity 'VACCINE' named entity 'HUMANS' named entity 'OUR' named entity 'HIV-1' named entity 'ROLE' named entity 'RECOVERED' named entity 'EPITOPE MAPPING' named entity 'MONOCLONAL ANTIBODY' named entity 'CHARACTERIZATION' named entity 'MANUSCRIPT' named entity 'SUSPECTED' named entity 'NUMBERING' named entity 'ENVELOPE PROTEIN'

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