|Title||Structural insight in the inhibition of adherence of F4 fimbriae producing enterotoxigenic Escherichia coli by llama single domain antibodies.|
|Publication Type||Journal Article|
|Year of Publication||2015|
|Authors||Moonens, K., I. Van den Broeck, E. Okello, E. Pardon, M. De Kerpel, H. Remaut, and H. De Greve|
|Date Published||2015 Feb 24|
|Keywords||Adhesins, Escherichia coli, Animals, Camelids, New World, Crystallography, X-Ray, Diarrhea, Enterotoxigenic Escherichia coli, Escherichia coli Infections, Fimbriae, Bacterial, Single-Domain Antibodies, Swine, Swine Diseases, Virus Shedding|
Enterotoxigenic Escherichia coli that cause neonatal and post-weaning diarrhea in piglets express F4 fimbriae to mediate attachment towards host receptors. Recently we described how llama single domain antibodies (VHHs) fused to IgA, produced in Arabidopsis thaliana seeds and fed to piglets resulted in a progressive decline in shedding of F4 positive ETEC bacteria. Here we present the structures of these inhibiting VHHs in complex with the major adhesive subunit FaeG. A conserved surface, distant from the lactose binding pocket, is targeted by these VHHs, highlighting the possibility of targeting epitopes on single-domain adhesins that are non-involved in receptor binding.
|Alternate Journal||Vet. Res.|
|PubMed Central ID||PMC4337312|
Structural insight in the inhibition of adherence of F4 fimbriae producing enterotoxigenic Escherichia coli by llama single domain antibodies.