9CCS
CryoEM Structure of Escherichia coli FimCH in complex with 2H04 Fab
Summary for 9CCS
| Entry DOI | 10.2210/pdb9ccs/pdb |
| EMDB information | 45456 |
| Descriptor | Type 1 fimbiral adhesin FimH, 2H04 Fab light chain, 2H04 Fab heavy chain (3 entities in total) |
| Functional Keywords | adhesin, inhibitor, complex, fab, chaperone, usher, pili, cell adhesion |
| Biological source | Escherichia coli UTI89 More |
| Total number of polymer chains | 3 |
| Total formula weight | 79324.18 |
| Authors | |
| Primary citation | Lopatto, E.D.B.,Santiago-Borges, J.M.,Sanick, D.A.,Malladi, S.K.,Azimzadeh, P.N.,Timm, M.W.,Fox, I.F.,Schmitz, A.J.,Turner, J.S.,Sayed Ahmed, S.M.,Ortinau, L.,Gualberto, N.C.,Pinkner, J.S.,Dodson, K.W.,Ellebedy, A.H.,Kau, A.L.,Hultgren, S.J. Monoclonal antibodies targeting the FimH adhesin protect against uropathogenic E. coli UTI. Sci Adv, 11:eadw0698-eadw0698, 2025 Cited by PubMed Abstract: As antimicrobial resistance increases, urinary tract infections (UTIs) are expected to pose an increased burden in morbidity and expense on the health care system, increasing the need for alternative antibiotic-sparing treatments. Most UTIs are caused by uropathogenic (UPEC), whereas causes a large portion of non-UPEC UTIs. Both bacteria express type 1 pili tipped with the mannose-binding FimH adhesin critical for UTI pathogenesis. We generated and biochemically characterized 33 murine monoclonal antibodies (mAbs) to FimH. Three mAbs protected mice from UTI. Mechanistically, we show that this protection is Fc independent and mediated by the ability of these mAbs to sterically block FimH function by recognizing a high-affinity FimH conformation. Our data reveal that FimH mAbs hold promise as an antibiotic-sparing treatment strategy. PubMed: 40540557DOI: 10.1126/sciadv.adw0698 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.17 Å) |
Structure validation
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