5D6C
Structure of 4497 Fab bound to synthetic wall teichoic acid fragment
Summary for 5D6C
| Entry DOI | 10.2210/pdb5d6c/pdb |
| Descriptor | 4497 antibody IgK (VL and CL), 4497 antibody IgG1 (VH and CH1), CALCIUM ION, ... (7 entities in total) |
| Functional Keywords | staphylococcus aureus wall teichoic acid antibody mrsa, immune system |
| Biological source | Homo sapiens More |
| Total number of polymer chains | 4 |
| Total formula weight | 97766.68 |
| Authors | Lupardus, P.J.,Fong, R. (deposition date: 2015-08-12, release date: 2015-11-11, Last modification date: 2024-10-30) |
| Primary citation | Lehar, S.M.,Pillow, T.,Xu, M.,Staben, L.,Kajihara, K.K.,Vandlen, R.,DePalatis, L.,Raab, H.,Hazenbos, W.L.,Morisaki, J.H.,Kim, J.,Park, S.,Darwish, M.,Lee, B.C.,Hernandez, H.,Loyet, K.M.,Lupardus, P.,Fong, R.,Yan, D.,Chalouni, C.,Luis, E.,Khalfin, Y.,Plise, E.,Cheong, J.,Lyssikatos, J.P.,Strandh, M.,Koefoed, K.,Andersen, P.S.,Flygare, J.A.,Wah Tan, M.,Brown, E.J.,Mariathasan, S. Novel antibody-antibiotic conjugate eliminates intracellular S. aureus. Nature, 527:323-328, 2015 Cited by PubMed Abstract: Staphylococcus aureus is considered to be an extracellular pathogen. However, survival of S. aureus within host cells may provide a reservoir relatively protected from antibiotics, thus enabling long-term colonization of the host and explaining clinical failures and relapses after antibiotic therapy. Here we confirm that intracellular reservoirs of S. aureus in mice comprise a virulent subset of bacteria that can establish infection even in the presence of vancomycin, and we introduce a novel therapeutic that effectively kills intracellular S. aureus. This antibody-antibiotic conjugate consists of an anti-S. aureus antibody conjugated to a highly efficacious antibiotic that is activated only after it is released in the proteolytic environment of the phagolysosome. The antibody-antibiotic conjugate is superior to vancomycin for treatment of bacteraemia and provides direct evidence that intracellular S. aureus represents an important component of invasive infections. PubMed: 26536114DOI: 10.1038/nature16057 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.72 Å) |
Structure validation
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