4WEU

Co-complex structure of the F4 fimbrial adhesin FaeG variant ad with llama single domain antibody V3

Summary for 4WEU

• Entry DOI: 10.2210/pdb4weu/pdb
• Related: 3HLR
• Descriptor: Anti-F4+ETEC bacteria VHH variable region, K88 fimbrial protein AD (3 entities in total)
• Functional Keywords: complex, adhesin, nanobody, llama single domain antibody, cell adhesion
• Biological source: Lama glama (Llama); More
• Cellular location: Fimbrium: P14191
• Total number of polymer chains: 4
• Total formula weight: 86520.01

Authors

Moonens, K.,Van den Broeck, I.,Pardon, E.,De Kerpel, M.,Remaut, H.,De Greve, H. (deposition date: 2014-09-11, release date: 2015-02-04, Last modification date: 2024-11-06)

Primary citation

Moonens, K.,Van den Broeck, I.,Okello, E.,Pardon, E.,De Kerpel, M.,Remaut, H.,De Greve, H.
Structural insight in the inhibition of adherence of F4 fimbriae producing enterotoxigenic Escherichia coli by llama single domain antibodies.
Vet. Res., 46:14-14, 2015

PubMed 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.

PubMed: 25828907
DOI: 10.1186/s13567-015-0151-x

Experimental method

X-RAY DIFFRACTION (2.61 Å)