Monoclonal antibodies from humans with Mycobacterium tuberculosis exposure or latent infection recognize distinct arabinomannan epitopes

<p>The surface polysacharide arabinomannan (AM) and related glycolipid lipoarabinomannan (LAM) play critical roles in tuberculosis pathogenesis. Human antibody responses to AM/LAM are heterogenous and knowledge of reactivity to specific glycan epitopes at the monoclonal level is limited, especially in individuals who can control <i><span>M. tuberculosis</span></i> infection<span>. </span>We generated human IgG mAbs to AM/LAM from B cells of two asymptomatic individuals exposed to or latently infected with <i><span>M. tuberculosis</span></i>. We here show that two of these mAbs have high affinity to AM/LAM, are non-competing, and recognize different glycan epitopes <span>distinct from other anti-AM/LAM mAbs reported. Both mAbs recognize virulent </span><i><span>M. tuberculosis</span></i><span> and nontuberculous mycobacteria with marked differences, can be used for the detection of urinary LAM, and can detect </span><i><span>M. tuberculosis</span></i><span> and LAM in infected lungs. These mAbs enhance our understanding of the spectrum of antibodies to AM/LAM epitopes </span>in humans <span>and</span> are valuable for <span>tuberculosis</span> diagnostic and research applications.</p>