4w6w | pdb_00004w6w

Co-complex structure of the lectin domain of F18 fimbrial adhesin FedF with inhibitory nanobody NbFedF6

spinqualitylabelsall models 4w6w, resolution 2.51Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4w6w is a 2 chain structure with sequence from Escherichia coli and Lama glama. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.51Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q47212_ECOLX Publication Abstract from PubMed Post-weaning diarrhea and edema disease caused by F18 fimbriated E. coli are important diseases in newly weaned piglets and lead to severe production losses in farming industry. Protective treatments against these infections have thus far limited efficacy. In this study we generated nanobodies directed against the lectin domain of the F18 fimbrial adhesin FedF and showed in an in vitro adherence assay that four unique nanobodies inhibit the attachment of F18 fimbriated E. coli bacteria to piglet enterocytes. Crystallization of the FedF lectin domain with the most potent inhibitory nanobodies revealed their mechanism of action. These either competed with the binding of the blood group antigen receptor on the FedF surface or induced a conformational change in which the CDR3 region of the nanobody displaces the D-E loop adjacent to the binding site. This D-E loop was previously shown to be required for the interaction between F18 fimbriated bacteria and blood group antigen receptors in a membrane context. This work demonstrates the feasibility of inhibiting the attachment of fimbriated pathogens by employing nanobodies directed against the adhesin domain. Nanobody Mediated Inhibition of Attachment of F18 Fimbriae Expressing Escherichia coli.,Moonens K, De Kerpel M, Coddens A, Cox E, Pardon E, Remaut H, De Greve H PLoS One. 2014 Dec 11;9(12):e114691. doi: 10.1371/journal.pone.0114691., eCollection 2014. PMID:25502211 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Adhesin 3D structures

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