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

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

PROVIDER: PRJNA1097646 | ENA |

REPOSITORIES: ENA

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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.

2024-06-01 | GSE263497 | GEO

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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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.

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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.

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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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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.

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