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

(2012) MOLECULAR MICROBIOLOGY. 86(1). p.82-95
Author
Organization
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.
Keywords
UROPATHOGENIC ESCHERICHIA-COLI, CHAPERONE-USHER PATHWAY, TAMM-HORSFALL PROTEIN, EDEMA DISEASE, URINARY-TRACT-INFECTION, RECEPTOR-BINDING, POSTWEANING DIARRHEA, CRYSTAL-STRUCTURE, VIRULENCE GENES, F107 FIMBRIAE

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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.
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.
Chicago author-date
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.
Chicago author-date (all authors)
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.
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.
IEEE
[1]
K. Moonens et al., “Structural insight in histo-blood group binding by the F18 fimbrial adhesin FedF,” MOLECULAR MICROBIOLOGY, vol. 86, no. 1, pp. 82–95, 2012.
@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},
  keywords     = {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},
}

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