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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
PMID:
25828907
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

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