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Structural insight in the inhibition of adherence of F4 fimbriae producing enterotoxigenic Escherichia coli by llama single domain antibodies

DOI: 10.1186/s13567-015-0151-x DOI Help
PMID: 25828907 PMID Help

Authors: Kristof Moonens (Vrije Universiteit Brussel) , Imke Van Den Broeck (Vrije Universiteit Brussel) , Emmanuel Okello (Vrije Universiteit Brussel) , Els Pardon (Vrije Universiteit Brussel) , Maia De Kerpel (Vrije Universiteit Brussel) , Han Remaut (Vrije Universiteit Brussel) , Henri De Greve (Vrije Universiteit Brussel)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Veterinary Research , VOL 46

State: Published (Approved)
Published: February 2015
Diamond Proposal Number(s): 9426

Open Access Open Access

Abstract: 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.

Subject Areas: Biology and Bio-materials


Instruments: I03-Macromolecular Crystallography

Other Facilities: SOLEIL