4WEM

Co-complex structure of the F4 fimbrial adhesin FaeG variant ac with llama single domain antibody V1

4WEM の概要

• エントリーDOI: 10.2210/pdb4wem/pdb
• 関連するPDBエントリー: 3HLR
• 分子名称: K88 fimbrial protein AC, Anti-F4+ETEC bacteria VHH variable region, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: complex, llama single domain antibody, adhesin, nanobody, structural protein
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 43062.34

構造登録者

Moonens, K.,Van den Broeck, I.,Pardon, E.,De Kerpel, M.,Remaut, H.,De Greve, H. (登録日: 2014-09-10, 公開日: 2015-02-04, 最終更新日: 2024-10-16)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.55 Å)