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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

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

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

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

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