8CR9
Cryo-EM structure of PcrV/Fab(30-B8)
Summary for 8CR9
| Entry DOI | 10.2210/pdb8cr9/pdb |
| EMDB information | 16805 |
| Descriptor | Heavy chain, light chain, Maltose/maltodextrin-binding periplasmic protein,Type III secretion protein PcrV (3 entities in total) |
| Functional Keywords | antibody t3ss tip protein, antimicrobial protein |
| Biological source | Homo sapiens More |
| Total number of polymer chains | 3 |
| Total formula weight | 122930.79 |
| Authors | |
| Primary citation | Simonis, A.,Kreer, C.,Albus, A.,Rox, K.,Yuan, B.,Holzmann, D.,Wilms, J.A.,Zuber, S.,Kottege, L.,Winter, S.,Meyer, M.,Schmitt, K.,Gruell, H.,Theobald, S.J.,Hellmann, A.M.,Meyer, C.,Ercanoglu, M.S.,Cramer, N.,Munder, A.,Hallek, M.,Fatkenheuer, G.,Koch, M.,Seifert, H.,Rietschel, E.,Marlovits, T.C.,van Koningsbruggen-Rietschel, S.,Klein, F.,Rybniker, J. Discovery of highly neutralizing human antibodies targeting Pseudomonas aeruginosa. Cell, 186:5098-5113.e19, 2023 Cited by PubMed Abstract: Drug-resistant Pseudomonas aeruginosa (PA) poses an emerging threat to human health with urgent need for alternative therapeutic approaches. Here, we deciphered the B cell and antibody response to the virulence-associated type III secretion system (T3SS) in a cohort of patients chronically infected with PA. Single-cell analytics revealed a diverse B cell receptor repertoire directed against the T3SS needle-tip protein PcrV, enabling the production of monoclonal antibodies (mAbs) abrogating T3SS-mediated cytotoxicity. Mechanistic studies involving cryoelectron microscopy identified a surface-exposed C-terminal PcrV epitope as the target of highly neutralizing mAbs with broad activity against drug-resistant PA isolates. These anti-PcrV mAbs were as effective as treatment with conventional antibiotics in vivo. Our study reveals that chronically infected patients represent a source of neutralizing antibodies, which can be exploited as therapeutics against PA. PubMed: 37918395DOI: 10.1016/j.cell.2023.10.002 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.2 Å) |
Structure validation
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