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

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

PROVIDER: PRJNA748441 | ENA |

REPOSITORIES: ENA

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

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 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.

2021-07-21 | GSE180517 | GEO

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.

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Deciphering Mycobacterium tuberculosis glycan epitopes through clustering of human polyclonal and isolating novel monoclonal antibodies II

Project description:The immunomodulatory mycobacterial surface antigen lipoarabinomannan (LAM) with its immunogenic glycan component arabinomannan (AM) facilitates Mycobacterium tuberculosis’ (Mtb) escape from the host’s immune response. Some but not all antibodies against AM can protect against TB. To better understand which of AM’s structures to target, we must first identify the spectrum of its epitopes. Through isolating and characterizing a panel of novel human mAbs with binding to distinct AM OS motifs, we further defined the glycan epitope structures, identified a new epitope, and determined their differences among mycobacterial strains.

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Deciphering Mycobacterium tuberculosis glycan epitopes through clustering of human polyclonal and isolating novel monoclonal antibodies I

Project description:The immunomodulatory mycobacterial surface antigen lipoarabinomannan (LAM) with its immunogenic glycan component arabinomannan (AM) facilitates Mycobacterium tuberculosis’ (Mtb) escape from the host’s immune response. Some but not all antibodies against AM can protect against TB. To better understand which of AM’s structures to target, we must first identify the spectrum of its epitopes. We here used synthetic AM oligosaccharide motifs to deplete sera from subjects along the spectrum of Mtb infection. Performing cluster analysis, we were able to predict AM’s immunogenic structures and delineate how antibody reactivity to them is influenced by Mtb infection states.

2024-06-01 | GSE263496 | GEO

Deciphering Mycobacterium tuberculosis glycan epitopes through clustering of human polyclonal and isolating novel monoclonal antibodies II

Project description:Deciphering Mycobacterium tuberculosis glycan epitopes through clustering of human polyclonal and isolating novel monoclonal antibodies II

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Deciphering Mycobacterium tuberculosis glycan epitopes through clustering of human polyclonal and isolating novel monoclonal antibodies I

Project description:Deciphering Mycobacterium tuberculosis glycan epitopes through clustering of human polyclonal and isolating novel monoclonal antibodies I

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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

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Pathogenic Natural Antibodies Recognizing Annexin IV Are Required to Develop Intestinal Ischemia-Reperfusion Injury

Project description:Intestinal ischemia-reperfusion (IR) injury is initiated when natural IgM antibodies recognize neo-epitopes that are revealed on ischemic cells. The target molecules and mechanisms whereby these neo-epitopes become accessible to recognition are not well understood. Proposing that isolated intestinal epithelial cells (IEC) may carry IR-related neo-epitopes, we used in vitro IEC binding assays to screen hybridomas created from B cells of unmanipulated wild type C57BL/6 mice. We identified a novel IgM monoclonal antibody (mAb B4) that reacted with the surface of IEC by flow cytometric analysis and was alone capable of causing complement activation, neutrophil recruitment and intestinal injury in otherwise IR-resistant Rag1-/- mice. Monoclonal Ab B4 was found to specifically recognize mouse annexin IV. Pre-injection of recombinant annexin IV blocked IR injury in wild type C57BL/6 mice, demonstrating the requirement for recognition of this protein in order to develop IR injury in the context of a complex natural antibody repertoire. Humans were also found to exhibit IgM natural antibodies that recognize annexin IV. These data in toto identify annexin IV as a key ischemia-related target antigen that is recognized by natural Abs in a pathologic process required in vivo to develop intestinal IR injury. Keywords: Natural antibodies, Annexin, Ischemia Reperfusion, Inflammation, Complement In the study presented here, a total of 4 custom spotted antigen slides were hybridized with known antibodies.

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Pathogenic Natural Antibodies Recognizing Annexin IV Are Required to Develop Intestinal Ischemia-Reperfusion Injury

2009-02-19 | GSE14862 | GEO