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Structural insight in histo-blood group binding by the F18 fimbrial adhesin FedF

Kristof Moonens, Julie Bouckaert, Annelies Coddens UGent, Thao Tran, Santosh Panjikar, Maia De Kerpel, Eric Cox UGent, Han Remaut and Henri De Greve (2012) MOLECULAR MICROBIOLOGY. 86(1). p.82-95
abstract
F18-positive enterotoxigenic and Shiga toxin-producing Escherichia coli are responsible for post-weaning diarrhoea and oedema disease in pigs and lead to severe production losses in the farming industry. F18 fimbriae attach to the small intestine of young piglets by latching onto glycosphingolipids with A/H blood group determinants on type 1 core. We demonstrate the N-terminal domain of the F18 fimbrial subunit FedF to be responsible for ABH-mediated attachment and present its X-ray structure in ligand-free form and bound to A and B type 1 hexaoses. The FedF lectin domain comprises a 10-stranded immunoglobulin-like beta-sandwich. Three linear motives, Q47-N50, H88-S90 and R117-T119, form a shallow glycan binding pocket near the tip of the domain that is selective for type 1 core glycans in extended conformation. In addition to the glycan binding pocket, a polybasic loop on the membrane proximal surface of FedF lectin domain is shown to be required for binding to piglet enterocytes. Although dispensable for ABH glycan recognition, the polybasic surface adds binding affinity in the context of the host cell membrane, a mechanism that is proposed to direct ABHglycan binding to cell-bound glycosphingolipids and could allow bacteria to avoid clearance by secreted glycoproteins.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
UROPATHOGENIC ESCHERICHIA-COLI, CHAPERONE-USHER PATHWAY, TAMM-HORSFALL PROTEIN, EDEMA DISEASE, URINARY-TRACT-INFECTION, RECEPTOR-BINDING, POSTWEANING DIARRHEA, CRYSTAL-STRUCTURE, VIRULENCE GENES, F107 FIMBRIAE
journal title
MOLECULAR MICROBIOLOGY
Mol. Microbiol.
volume
86
issue
1
pages
82 - 95
Web of Science type
Article
Web of Science id
000309063600009
JCR category
MICROBIOLOGY
JCR impact factor
4.961 (2012)
JCR rank
19/116 (2012)
JCR quartile
1 (2012)
ISSN
0950-382X
DOI
10.1111/j.1365-2958.2012.08174.x
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
3052456
handle
http://hdl.handle.net/1854/LU-3052456
date created
2012-11-13 15:45:16
date last changed
2012-11-14 08:31:52
@article{3052456,
  abstract     = {F18-positive enterotoxigenic and Shiga toxin-producing Escherichia coli are responsible for post-weaning diarrhoea and oedema disease in pigs and lead to severe production losses in the farming industry. F18 fimbriae attach to the small intestine of young piglets by latching onto glycosphingolipids with A/H blood group determinants on type 1 core. We demonstrate the N-terminal domain of the F18 fimbrial subunit FedF to be responsible for ABH-mediated attachment and present its X-ray structure in ligand-free form and bound to A and B type 1 hexaoses. The FedF lectin domain comprises a 10-stranded immunoglobulin-like beta-sandwich. Three linear motives, Q47-N50, H88-S90 and R117-T119, form a shallow glycan binding pocket near the tip of the domain that is selective for type 1 core glycans in extended conformation. In addition to the glycan binding pocket, a polybasic loop on the membrane proximal surface of FedF lectin domain is shown to be required for binding to piglet enterocytes. Although dispensable for ABH glycan recognition, the polybasic surface adds binding affinity in the context of the host cell membrane, a mechanism that is proposed to direct ABHglycan binding to cell-bound glycosphingolipids and could allow bacteria to avoid clearance by secreted glycoproteins.},
  author       = {Moonens, Kristof and Bouckaert, Julie and Coddens, Annelies and Tran, Thao and Panjikar, Santosh and De Kerpel, Maia and Cox, Eric and Remaut, Han and De Greve, Henri},
  issn         = {0950-382X},
  journal      = {MOLECULAR MICROBIOLOGY},
  keyword      = {UROPATHOGENIC ESCHERICHIA-COLI,CHAPERONE-USHER PATHWAY,TAMM-HORSFALL PROTEIN,EDEMA DISEASE,URINARY-TRACT-INFECTION,RECEPTOR-BINDING,POSTWEANING DIARRHEA,CRYSTAL-STRUCTURE,VIRULENCE GENES,F107 FIMBRIAE},
  language     = {eng},
  number       = {1},
  pages        = {82--95},
  title        = {Structural insight in histo-blood group binding by the F18 fimbrial adhesin FedF},
  url          = {http://dx.doi.org/10.1111/j.1365-2958.2012.08174.x},
  volume       = {86},
  year         = {2012},
}

Chicago
Moonens, Kristof, Julie Bouckaert, Annelies Coddens, Thao Tran, Santosh Panjikar, Maia De Kerpel, Eric Cox, Han Remaut, and Henri De Greve. 2012. “Structural Insight in Histo-blood Group Binding by the F18 Fimbrial Adhesin FedF.” Molecular Microbiology 86 (1): 82–95.
APA
Moonens, K., Bouckaert, J., Coddens, A., Tran, T., Panjikar, S., De Kerpel, M., Cox, E., et al. (2012). Structural insight in histo-blood group binding by the F18 fimbrial adhesin FedF. MOLECULAR MICROBIOLOGY, 86(1), 82–95.
Vancouver
1.
Moonens K, Bouckaert J, Coddens A, Tran T, Panjikar S, De Kerpel M, et al. Structural insight in histo-blood group binding by the F18 fimbrial adhesin FedF. MOLECULAR MICROBIOLOGY. 2012;86(1):82–95.
MLA
Moonens, Kristof, Julie Bouckaert, Annelies Coddens, et al. “Structural Insight in Histo-blood Group Binding by the F18 Fimbrial Adhesin FedF.” MOLECULAR MICROBIOLOGY 86.1 (2012): 82–95. Print.