by Keyword: Immunoglobulin g
Drainas AP, McIlwain DR, Dallas A, Chu T, Delgado-González A, Baron M, Angulo-Ibáñez M, Trejo A, Bai Y, Hickey JW, Lu G, Lu S, Pineda-Ramirez J, Anglin K, Richardson ET, Prostko JC, Frias E, Servellita V, Brazer N, Chiu CY, Peluso MJ, Martin JN, Wirz OF, Pham TD, Boyd SD, Kelly JD, Sage J, Nolan GP, Rovira-Clavé X, (2025). High-throughput multiplexed serology via the mass-spectrometric analysis of isotopically barcoded beads Nature Biomedical Engineering 9, 1117-1128 
In serology, each sample is typically tested individually, one antigen at a time. This is costly and time consuming. Serology techniques should ideally allow recurrent measurements in parallel in small sample volumes and be inexpensive and fast. Here we show that mass cytometry can be used to scale up multiplexed serology testing by leveraging polystyrene beads uniformly loaded with combinations of stable isotopes. We generated 18,480 unique isotopically barcoded beads to simultaneously detect, in a single tube with 924 serum samples, the levels of immunoglobulins G and M against 19 proteins from SARS-CoV-2 (a total of 36,960 tests in 400 nl of sample volume and 30 mu l of reaction volume). As a rapid, high-throughput and cost-effective technique, serology by mass cytometry may contribute to the effective management of public health emergencies originating from infectious diseases.
JTD Keywords: Antibodies, viral, Biolog, Covid-19, Covid-19 serological testing, Cytometer, High-throughput screening assays, Humans, Immunoglobulin g, Immunoglobulin m, Mass spectrometry, Microspheres, Polystyrenes, Sars-cov-2, Transmission
Marti, D, Martin-Martinez, E, Torras, J, Bertran, O, Turon, P, Aleman, C, (2021). In silico antibody engineering for SARS-CoV-2 detection Computational And Structural Biotechnology Journal 19, 5525-5534
Engineered immunoglobulin-G molecules (IgGs) are of wide interest for the development of detection elements in protein-based biosensors with clinical applications. The strategy usually employed for the de novo design of such engineered IgGs consists on merging fragments of the three-dimensional structure of a native IgG, which is immobilized on the biosensor surface, and of an antibody with an exquisite target specificity and affinity. In this work conventional and accelerated classical molecular dynamics (cMD and aMD, respectively) simulations have been used to propose two IgG-like antibodies for COVID-19 detection. More specifically, the crystal structure of the IgG1 B12 antibody, which inactivates the human immunodeficiency virus-1, has been merged with the structure of the antibody CR3022 Fab tightly bounded to SARS-CoV-2 receptor-binding domain (RBD) and the structure of the 5309 antibody Fab fragment complexed with SARS-CoV-2 RBD. The two constructed antibodies, named IgG1-CR3022 and IgG1-S309, respectively, have been immobilized on a stable gold surface through a linker. Analyses of the influence of both the merging strategy and the substrate on the stability of the two constructs indicate that the IgG1-S309 antibody better preserves the neutralizing structure than the IgG1-CR3022 one. Overall, results indicate that the IgG1-S309 is appropriated for the generation of antibody based sensors for COVID-19 diagnosis. (C) 2021 The Author(s). Published by Elsevier B.V. on behalf of Research Network of Computational and Structural Biotechnology.
JTD Keywords: cr3022, igg1, molecular engineering, s309, Antibodies, Antibody engineering, Biosensors, Chemical detection, Clinical application, Cov, Cr3022, Crystal structure, Design, Diseases, Gold nanoparticles, Igg1, Igg1 antibody, Immobilization, Immunoglobulin g, Immunosensor, In-silico, Merging, Molecular dynamics, Molecular engineering, Orientation, Protein-based biosensors, Receptor-binding domains, S309, Sars, Sensor, Spike protein, Target, Vaccine, Viruses
