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9MKN

Structure of the Respiratory Syncytial Virus Fusion Protein Bound to Human Antibodies RSV_2245 and RSV_3301

Summary for 9MKN
Entry DOI10.2210/pdb9mkn/pdb
EMDB information48331
DescriptorFusion glycoprotein F2, Fusion glycoprotein F1, 2245 Fab Heavy Chain, ... (6 entities in total)
Functional Keywordsfusion protein, trimer, antibody, complex, antiviral protein, viral protein-immune system complex, viral protein/immune system
Biological sourceRespiratory syncytial virus
More
Total number of polymer chains18
Total formula weight434849.69
Authors
Johnson, N.V.,McLellan, J.S. (deposition date: 2024-12-17, release date: 2025-10-29, Last modification date: 2025-12-24)
Primary citationWasdin, P.T.,Johnson, N.V.,Janke, A.K.,Held, S.,Marinov, T.M.,Jordaan, G.,Gillespie, R.A.,Vandenabeele, L.,Pantouli, F.,Powers, O.C.,Vukovich, M.J.,Holt, C.M.,Kim, J.,Hansman, G.,Logue, J.,Chu, H.Y.,Andrews, S.F.,Kanekiyo, M.,Sautto, G.A.,Ross, T.M.,Sheward, D.J.,McLellan, J.S.,Abu-Shmais, A.A.,Georgiev, I.S.
Generation of antigen-specific paired-chain antibodies using large language models.
Cell, 188:7206-, 2025
Cited by
PubMed Abstract: The traditional process of antibody discovery is limited by inefficiency, high costs, and low success rates. Recent approaches employing artificial intelligence (AI) have been developed to optimize existing antibodies and generate antibody sequences in a target-agnostic manner. In this work, we present MAGE (monoclonal antibody generator), a sequence-based protein language model (PLM) fine-tuned for the task of generating paired human variable heavy- and light-chain antibody sequences against targets of interest. We show that MAGE can generate novel and diverse antibody sequences with experimentally validated binding specificity against SARS-CoV-2, an emerging avian influenza H5N1, and respiratory syncytial virus A (RSV-A). MAGE represents a first-in-class model capable of designing human antibodies against multiple targets with no starting template.
PubMed: 41192421
DOI: 10.1016/j.cell.2025.10.006
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.4 Å)
Structure validation

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PDB entries from 2025-12-31

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