Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Prediction of broadly neutralizing antibodies [10X]

ABSTRACT: We generated the humoral immune repertoire of circulating memory B cells from healthy and HIV infected immune donors. These repertoires were used to predict specific HIV antibodies directed against gp120/gp41.

ORGANISM(S): Homo sapiens

PROVIDER: GSE228912 | GEO | 2024/06/04

REPOSITORIES: GEO

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
		Other

Items per page:

1 - 1 of 1

Similar Datasets

Prediction of broadly neutralizing antibodies [Singleron]

Project description:We generated the humoral immune repertoire of circulating memory B cells from healthy and HIV infected immune donors. These repertoires were used to predict specific HIV antibodies directed against gp120/gp41.

2024-06-04 | GSE229122 | GEO

Prediction of broadly neutralizing antibodies [BD Rhapsody]

2024-06-04 | GSE229121 | GEO

Identification of autoantigens recognized by the 2F5 and 4E10 broadly neutralizing HIV-1 antibodies

Project description:Many human monoclonal antibodies that neutralize multiple clades of HIV-1 are polyreactive and bind avidly to mammalian autoantigens. Indeed, the generation of neutralizing antibodies to the 2F5 and 4E10 epitopes of HIV-1 gp41 in man may be proscribed by immune tolerance since mice expressing the VH and VL regions of 2F5 have a block in B-cell development characteristic of central tolerance. This developmental blockade implies the presence of tolerizing autoantigens that are mimicked by the membrane-proximal external region of HIV-1 gp41. Here we identify human kynureninase (KYNU) and splicing factor 3b subunit 3 (SF3B3) as the primary conserved, vertebrate self-antigens recognized by the 2F5 and 4E10 antibodies, respectively. 2F5 binds the H4 domain of KYNU which contains the complete 2F5 linear epitope (ELDKWA). 4E10 recognizes a conformational epitope of SF3B3 that is strongly dependent on hydrophobic interactions. Opossums carry a rare KYNU H4 domain that abolishes 2F5 binding, but retain all SF3B3 4E10 epitopes. Immunization of opossums with HIV-1 gp140 induced extraordinary titers of serum antibody to the 2F5 ELDKWA epitope but little or nothing to the 4E10 determinant. Identification of structural motif shared by vertebrates and HIV-1 provides direct evidence that immunological tolerance can impair humoral responses to HIV-1. The invitrogen protoarray that contains >9,400 recombinant human proteins was used to identify self-ligands that are recognized by broadly neutralizing HIV-1 antibodies 2F5 and 4E10. An isotype-matched human myeloma protein (151K, Southern Biotech) was used as control.

2012-12-03 | E-GEOD-42673 | biostudies-arrayexpress

Identification of autoantigens recognized by the 2F5 and 4E10 broadly neutralizing HIV-1 antibodies

2012-12-03 | GSE42673 | GEO

Prediction of broadly neutralizing antibodies

Project description:This SuperSeries is composed of the SubSeries listed below.

2024-06-04 | GSE229123 | GEO

A high throughput protein microarray approach to classify HIV monoclonal antibodies and variant antigens

Project description:In recent years, high throughput discovery of human recombinant monoclonal antibodies (mAbs) has been applied, to greatly advance our understanding of the specificity, and functional activity of antibodies, against HIV. Thousands of antibodies have been generated and screened in functional neutralization assays, and antibodies, associated with cross-strain neutralization and passive protection in primates, have been identified. To facilitate this type of discovery, a high throughput-screening tool is needed, to accurately classify mAbs, and their antigen targets. In this study, we analyzed and evaluated a prototype microarray chip, comprised of HIV-1 recombinant proteins gp140, gp120, gp41, and several membrane proximal external region peptides. The protein microarray analysis of 11 HIV-1 envelope-specific mAbs revealed diverse binding affinities and specificities across clades. Half maximal effective concentrations, generated by our chip analysis, correlated significantly (P<0.0001) with concentrations from ELISA binding measurements. Polyclonal immune responses in plasma samples, from HIV-1 infected subjects, exhibited different binding patterns and reactivity against printed proteins. Examining the totality of the specificity of the humoral response in this way reveals the exquisite diversity, and specificity of the humoral response to HIV.

2015-03-10 | GSE66659 | GEO

HIV-1 gp120 impairs B cell proliferation by inducing TGF-β1 production and FcRL4 expression via an α4β7-dependent mechanism

Project description:The anti-HIV humoral immune response following acute infection is delayed and ineffective. HIV envelope protein gp120 binds to and signals through α4β7 on T cells. We show that gp120 also binds and signals through α4β7 on B cells, resulting in an abortive proliferative response. In primary B cells, gp120 signaling through α4β7 resulted in increased expression of TGF-β1 and the B cell inhibitory receptor FcRL4. Co-culture of B cells with HIV-infected autologous CD4+ T cells also resulted in increased B cell FcRL4 expression. These findings indicate that, in addition to inducing chronic immune activation, viral proteins can contribute directly to HIV-associated B cell dysfunction, thus providing a mechanism whereby the virus subverts the early HIV-specific humoral immune response. Forty-two samples in two batches were run with different treatments and different time points.

2013-10-17 | E-GEOD-49019 | biostudies-arrayexpress

HIV-1 gp120 impairs B cell proliferation by inducing TGF-β1 production and FcRL4 expression via an α4β7-dependent mechanism

2013-10-17 | GSE49019 | GEO

Afucosylated broadly neutralizing antibodies enhance clearance of HIV-1 infected cells through NK cell mediated killing

Project description:A series of monoclonal antibodies (mAbs) against human immune deficiency virus (HIV) were prepared utilizing different variable regions targeting HIV epitopes in combination with glycoengineering to produce mAbs with low Fc fucosylation. This dataset pertains to the Fc N-glycosylation analysis of these mAbs.

2024-07-30 | PXD053363 | Pride

Variability in the Glycosylation Patterns of gp120 Proteins from Different Human Immunodeficiency Virus Type 1 Isolates Expressed in Different Host Cells

Project description:The mature HIV-1 envelope (Env) glycoprotein is composed of gp120, the exterior subunit, and gp41, the transmembrane subunit assembled as trimer by noncovalent interaction. There is a great body of literature to prove that gp120 binds to CD4 first, then to the co-receptor. We have recently demonstrated that gp120 cannot bind to the co-receptor without first interacting with CD4. Previous studies provided different glycomic maps for the HIV-1 gp120. Here, we build on previous work to report that the use of LC-MS/MS, in conjunction with hydrophilic interaction liquid chromatography (HILIC) enrichment to glycosylation sites, is associated with the assorted neutralizing or binding events of glycosylation targeted antibodies from different clades or strains. In this study, the microheterogeneity of the glycosylation from 4 different clades of gp120s is deeply investigated. Aberrant glycosylation patterns were detected on gp120 originated from different clades, viral sequences and host cells. The results of this study may help provide better understanding of the mechanism of how the glycans participate in antibody neutralizing process that target glycosylation sites.

2021-11-01 | PXD027353 | Pride

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data