Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Human monoclonal antibodies to M. tuberculosis arabinomannan recognize distinct glycan epitopes - implications for TB diagnostics and research

ABSTRACT: Human antibody responses to AM/LAM are heterogenous and knowledge of reactivity to specific glycan epitopes at the monoclonal level is limited. Using novel glycan arrays, we characterized very high affinity monoclonal antibodies to AM/LAM, determined these mAbs are non-competing, and recognized distinct glycan epitopes. distinct from other anti-AM/LAM mAbs reported.

ORGANISM(S): synthetic construct Mus musculus Homo sapiens

PROVIDER: GSE180517 | GEO | 2021/07/21

REPOSITORIES: GEO

ACCESS DATA

Json Xml

Similar Datasets

Features and protective efficacy of human monoclonal antibodies targeting M. tuberculosis arabinomannan

Project description:Human antibody responses to AM/LAM are heterogenous and knowledge of reactivity to specific glycan epitopes at the monoclonal level is limited. Using novel glycan arrays, we characterized a very high affinity monoclonal antibody P1AM25 to AM/LAM, determined this mAb recognized distinct glycan epitopes from other anti-AM/LAM mAbs reported.

2023-11-08 | GSE218873 | GEO

Human monoclonal antibodies to M. tuberculosis arabinomannan recognize distinct glycan epitopes - implications for TB diagnostics and research

Project description:Human monoclonal antibodies to M. tuberculosis arabinomannan recognize distinct glycan epitopes - implications for TB diagnostics and research

| PRJNA748441 | ENA

Gluten-specific antibodies of celiac disease gut plasma cells recognize long proteolytic fragments that typically harbor T-cell epitopes

Project description:This study aimed to identify proteolytic fragments of gluten proteins recognized by recombinant IgG1 monoclonal antibodies generated from single IgA plasma cells of celiac disease lesions. Peptides bound by monoclonal antibodies in complex gut-enzyme digests of gluten treated with the deamidating enzyme transglutaminase 2, were identified by mass spectrometry after antibody pull-down with protein G beads. The antibody bound peptides were long deamidated peptide fragments that contained the substrate recognition sequence of transglutaminase 2. Characteristically, the fragments contained epitopes with the sequence QPEQPFP and variants thereof in multiple copies, and they typically also harbored many different gluten T-cell epitopes. In the pull-down setting where antibodies were immobilized on a solid phase, peptide fragments with multivalent display of epitopes were targeted. This scenario resembles the situation of the B-cell receptor on the surface of B cells. Conceivably, B cells of celiac disease patients select gluten epitopes that are repeated multiple times in long peptide fragments generated by gut digestive enzymes. As the fragments also contain many different T-cell epitopes, this will lead to generation of strong antibody responses by effective presentation of several distinct T-cell epitopes and establishment of T-cell help to B cells.

2016-05-10 | PXD002678 | Pride

Capsular glycan recognition provides antibody-mediated protection against tuberculosis

Project description:Increasing evidence suggests that antibodies (Abs) can have protective roles in M. tuberculosis (Mtb) infection but knowledge of the most relevant protective antigens and epitopes in humans is limited. Using novel glycan arrays, we establish that human serum IgG induced against the M. tuberculosis (Mtb) capsular polysacharide arabinomannan (AM) in natural Mtb infection is highly heterogeneous in its binding specificity and differs in both its reactivity to oligosaccharide (OS) motifs within AM and its functions between BCG vaccination and/or controlled (latent) versus uncontrolled (TB) M. tuberculosis infection. We show that anti-AM IgG from asymptomatic but not diseased individuals is protective, and provide data suggesting a role of IgG2 and specific AM oligosaccharides. Filling a gap in the current knowledge of protective antigens in humans, our human data support the key role of the M. tuberculosis surface glycan AM and suggest the importance of targeting specific glycan epitopes within AM in antibody-mediated immunity against TB.

2019-12-10 | GSE141679 | GEO

monoclonal antibody NIST8671 LC-MS/MS

Project description:The characteristics of monoclonal antibodies (mAbs) cohering various function effectors shows great expectation in therapy. Glycosylation, one of the common post-translational modifications, deeply influences the cohesion. It is necessary to grasp monosaccharide composition/sequence and glycan structures in mAbs. There have been comprehensive mass spectrometry characterization of N-glycosylation of mAbs, and monosaccharide compositions are deduced according to known biosynthetic rules. Our recently developed intact N-glycopeptide search engine GPSeeker has made unambiuous structure-specific characterization of N-glycosylation possible with structure-diagnostic fragment ions from selective fragmentattion of N-glycan moieties.

2022-04-14 | PXD032275 | Pride

SUGAR-Seq enables simultaneous detection of glycans, epitopes and the transcriptome in single cells [ATAC-seq]

Project description:Multi-modal single cell RNA sequencing enables the precise mapping of transcriptional and phenotypic features of cellular differentiation states, but does not allow for simultaneous integration of critical post-translational modification data. Here, we describe SUrface-protein Glycan And RNA-seq (SUGAR-seq); a method that enables detection and analysis of N-linked glycosylation, extracellular epitopes and the transcriptome at the single cell level. Integrated SUGAR-seq and glycoproteome analysis identified tumor infiltrating T cells with unique surface glycan properties that report their epigenetic and functional state.

2021-02-22 | GSE166324 | GEO

Gluten-specific antibodies of celiac disease gut plasma cells recognize long proteolytic fragments that typically harbor T-cell epitopes

2017-03-29 | MSV000080779 | MassIVE

SUGAR-Seq enables simultaneous detection of glycans, epitopes and the transcriptome in single cells [TIL scRNA-seq]

2021-02-22 | GSE166326 | GEO

SUGAR-Seq enables simultaneous detection of glycans, epitopes and the transcriptome in single cells [LN scRNA-seq]

2021-02-22 | GSE166325 | GEO

SUGAR-Seq enables simultaneous detection of glycans, epitopes and the transcriptome in single cells [3'RNA-seq]

2021-02-22 | GSE166323 | GEO