The only currently commercialized point-of-care assay for tuberculosis (TB) that measures lipoarabinomannan (LAM) in urine (Alere LF-LAM) has insufficient sensitivity. We evaluated the potential of 100 novel monoclonal antibody pairs targeting a variety of LAM epitopes on a sensitive electrochemiluminescence platform to improve the diagnostic accuracy.

Oriented "shish-kebab" structure can enable remarkable mechanical enhancement in polymers. Therefore, the formation mechanism and practical application of this structure have been extensively studied. However, the effect of shish-kebab content on mechanical properties is still uncertain. Knowledge of this effect is crucial in the academic and industrial fields but remains elusive because shish-kebab content is difficult to control. In this work, a self-developed multiflow vibrateinjection molding was used to produce samples with different shear layer thicknesses. The content of shish-kebab was represented by R, i.e., the thickness ratio of shear layer (composed by shish-kebab) to the whole sample. Results showed that with increased R impact/tensile strength exponentially increased, whereas elongation at break exponentially decreased. Based on the results, a modified model was proposed to interpret the strengthening and toughening mechanism. This study established a new method of predicting and controlling the mechanical properties of samples with shish-kebab and spherulite structures.

Lipoarabinomannan (LAM), the major antigenic glycolipid of Mycobacterium tuberculosis, is an important immunodiagnostic target for detecting tuberculosis (TB) infection in HIV-1–coinfected patients, and is believed to mediate a number of functions that promote infection and disease development. To probe the human humoral response against LAM during TB infection, several novel LAM-specific human mAbs were molecularly cloned from memory B cells isolated from infected patients and grown in vitro. The fine epitope specificities of these Abs, along with those of a panel of previously described murine and phage-derived LAM-specific mAbs, were mapped using binding assays against LAM Ags from several mycobacterial species and a panel of synthetic glycans and glycoconjugates that represented diverse carbohydrate structures present in LAM. Multiple reactivity patterns were seen that differed in their specificity for LAM from different species, as well as in their dependence on arabinofuranoside branching and nature of capping at the nonreducing termini. Competition studies with mAbs and soluble glycans further defined these epitope specificities and guided the design of highly sensitive immunodetection assays capable of detecting LAM in urine of TB patients, even in the absence of HIV-1 coinfection. These results highlighted the complexity of the antigenic structure of LAM and the diversity of the natural Ab response against this target. The information and novel reagents described in this study will allow further optimization of diagnostic assays for LAM and may facilitate the development of potential immunotherapeutic approaches to inhibit the functional activities of specific structural motifs in LAM.