Michael J Taussig's research while affiliated with Babraham Institute and other places

... The international community has also come up with a proposal called Minimum Information About a Protein Affinity Reagent (MIAPAR), which aims to establish a stronger connection between antibody producers and users. MIAPAR-compliant data include information such as the production/purification process, experimental evidence, updated protocols, and other relevant details (7,9). ...

... Extrapolating from a structural analysis of the placental AP, a model for the protein structure of TNAP was developed, which implies that the enzyme contains two Zn 2+ ions and one Mg 2+ ion in its active center [9]. The function of an additionally identified Ca 2+ site is still unclear [10]. ...

... In the last years, it became evident that biologics have a broad potential in a number of medical indication area like oncology or inflammation. [1] As parenterals, most biologics are applied as infusions or via the sub-cutaneous route. [2,3] The necessary dosages of antibody biologics are often very high, reaching amounts of up to several 100 of milligrams per application. As a consequence, protein concentrations >100 mg/mL are required for sub-cutaneous application. For example, I ...

... An alternative strategy in such cases has been the use of biomolecular scaffolds that can incorporate the properties of the receptor binding site. mAbs are prime candidates for such a role since their affinity and specificity can be naturally tailored and have indeed been used in varied scenarios to elucidate functionally relevant ligand-receptor interactions, constrain flexible molecules in their biologically active forms [21,22] and in few cases capture metabolites in their transition states [23]. Earlier studies from our laboratory demonstrated that an otherwise flexible peptide antigen could be held in a single conformation by three independent mAbs [24]. ...

... For instance, the Fc fraction of IgG, which rheumatoid factor targets, contains multiple 'SSV' motifs, which we also observed in peptides preferentially bound in older donors. While rheumatoid factor doesn't bind these motifs in co-crystals with IgG Fc (primarily binding to CH2 and CH3 domains) [43,44], it is intriguing that multiple diserine motifs may stabilize interaction to enhance autoantibody avidity. ...

... Ribosome display is a cell-free method that overcomes some of limitations in phage display technique such as transformation steps which increases library capability [9] or enable expression of toxic proteins without affecting growth rate of the host [10][11][12][13]. Ribosome display, as a rapid and robust technique, was first used by Hanes and Plueckthun [14,15], simultaneously by He and Taussig [16], for affinity selection of single chain antibodies. Thereafter, it has been widely used for in vitro selection of different functional molecules (scFvs, sdAbs, DARPins, Affibodies, etc.) against targets of interest [17][18][19][20][21][22][23][24][25][26][27][28][29][30][31] and also for affinity maturation of phage displayed selected binders [17,[32][33][34]. ...

... The proteins once expressed become rapidly immobilized on the capture slide, creating a protein array that can be duplicated several times. DAPA has been extended to print arrays of 116 different proteins (Stoevesandt, Vetter et al. 2011). It has also been optimized using different array support coatings, which increase its sensitivity towards the printed proteins (Schmidt, Cook et al. 2013). ...

... In fact, Hopp and Woods assigns R, K, D, E, and Q as amino acids with the highest hydrophilicity index values [26]. Other investigators are aware of the immunogenic nature of these side chains [27] and PE was partially deimmunized by mutating combinations of only these residues [7]. Thus, using the known X-ray crystallographic structure of DT390, we identified 24 potential amino acids (R, K, D, E, and Q) located in prominent positions on the molecular surface. ...

... Many of the conventional antibody/antigen-based ELISA-based assays are highly speci c, however, they lack the level of sensitivity needed for detection of disease at an early stage. One of the main reasons is poor or insu cient alignment and distribution of the antibodies on the sensor substrate that limits the number of antibody-antigen binding events 18 . To address this challenge nanoparticles (NPs) have been used to effectively in regulate the alignment and distribution of antibodies on its surface to enhance sensitivity and improve interaction with the substrate. ...

... Indeed, in mice in which both Ig-κ and Ig-λ are ablated, there is almost a complete lack of mature B cells [59]. The only LC-less B cells that do survive express at the cell surface HC, in which the C H 1 domain is deleted [60], highlighting that the C H 1 domain is key for ER retention of the HC, and for eliciting (UPR-driven) HC toxicity, which is in line with our findings in the HeLa-μ s model [9]. Also the recombination and SHM of the Ig-κ or Ig-λ locus often result in aberrant LCs that provoke proteotoxic ER stress [61], which, analogously, could be co-opted as a counter-selection criterion for defective B cell clones. ...