8BE1
SARS-CoV-2 RBD in complex with a Fab fragment of a neutralising antibody mRBD2
Summary for 8BE1
| Entry DOI | 10.2210/pdb8be1/pdb |
| Descriptor | Antibody heavy chain, Antibody light chain, Spike protein S1, ... (5 entities in total) |
| Functional Keywords | fab, antibody, sars-cov-2, rbd, neutralising, immune system |
| Biological source | Mus musculus More |
| Total number of polymer chains | 6 |
| Total formula weight | 143300.64 |
| Authors | Lulla, A.,Brear, P.,Fischer, K.,Hollfelder, F.,Hyvonen, M. (deposition date: 2022-10-21, release date: 2023-01-25, Last modification date: 2026-05-13) |
| Primary citation | Fischer, K.,Lulla, A.,So, T.Y.,Pereyra-Gerber, P.,Raybould, M.I.J.,Kohler, T.N.,Yam-Puc, J.C.,Kaminski, T.S.,Hughes, R.,Pyeatt, G.L.,Leiss-Maier, F.,Brear, P.,Matheson, N.J.,Deane, C.M.,Hyvonen, M.,Thaventhiran, J.E.D.,Hollfelder, F. Rapid discovery of monoclonal antibodies by microfluidics-enabled FACS of single pathogen-specific antibody-secreting cells. Nat.Biotechnol., 43:960-970, 2025 Cited by PubMed Abstract: Monoclonal antibodies are increasingly used to prevent and treat viral infections and are pivotal in pandemic response efforts. Antibody-secreting cells (ASCs; plasma cells and plasmablasts) are an excellent source of high-affinity antibodies with therapeutic potential. Current methods to study antigen-specific ASCs either have low throughput, require expensive and labor-intensive screening or are technically demanding and therefore not widely accessible. Here we present a straightforward technology for the rapid discovery of monoclonal antibodies from ASCs. Our approach combines microfluidic encapsulation of single cells into an antibody capture hydrogel with antigen bait sorting by conventional flow cytometry. With our technology, we screened millions of mouse and human ASCs and obtained monoclonal antibodies against severe acute respiratory syndrome coronavirus 2 with high affinity (<1 pM) and neutralizing capacity (<100 ng ml) in 2 weeks with a high hit rate (>85% of characterized antibodies bound the target). By facilitating access to the underexplored ASC compartment, the approach enables efficient antibody discovery and immunological studies into the generation of protective antibodies. PubMed: 39143416DOI: 10.1038/s41587-024-02346-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.98 Å) |
Structure validation
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