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Structural and adhesive properties of the long polar fimbriae protein LpfD from adherent-invasive Escherichia coli

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Abstract
Crohn's disease (CD) is an inflammatory bowel disease characterized by an exaggerated immune response to commensal microbiota in the intestines of patients. Metagenomic studies have identified specific bacterial species and strains with increased prevalence in CD patients, amongst which is the adherent-invasive Escherichia coli (AIEC) strain LF82. AIEC strains express long polar fimbriae (LPF), which are known to target Peyer's patches in a mouse CD model. Here, the recombinant production of a soluble, self-complemented construct of the LpfD protein of E. coli LF82 is reported and it is demonstrated that it forms the adhesive tip subunit of LPF. The LpfD crystal reveals an N-terminal adhesin domain and a C-terminal pilin domain that connects the adhesin to the minor pilus subunit LpfE. Surface topology and sequence conservation in the adhesin domain hint at a putative receptor-binding pocket as found in the Klebsiella pneumoniae MrkD and E. coli F17-G (GafD) adhesins. Immunohistostaining of murine intestinal tissue sections revealed that LpfD specifically binds to the intestinal mucosa and submucosa. LpfD binding was found to be resistant to treatment with O- or N-glycosidases, but was lost in collagenase-treated tissue sections, indicating the possible involvement of an intestinal matrix-associated protein as the LpfD receptor. LpfD strongly adhered to isolated fibronectin in an in vitro assay, and showed lower levels of binding to collagen V and laminin and no binding to collagens I, III and IV.
Keywords
LpfD, cell adhesion, Crohn's disease, bacterial adhesion, fimbrial adhesin, INFLAMMATORY-BOWEL-DISEASE, EXTRACELLULAR-MATRIX PROTEINS, INTESTINAL EPITHELIAL-CELLS, DRIVES FIBER FORMATION, CROHNS-DISEASE, ILEAL MUCOSA, SALMONELLA-TYPHIMURIUM, MECHANICAL FORCE, TYPE-3 FIMBRIAE, WEB SERVICES

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Citation

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Chicago
Coppens, Fanny, Jegan Iyyathurai, Segolène Ruer, Antonella Fioravanti, Joemar Taganna, Lars Vereecke, Henri De Greve, and Han Remaut. 2015. “Structural and Adhesive Properties of the Long Polar Fimbriae Protein LpfD from Adherent-invasive Escherichia Coli.” Acta Crystallographica Section D-biological Crystallography 71 (8): 1615–1626.
APA
Coppens, Fanny, Iyyathurai, J., Ruer, S., Fioravanti, A., Taganna, J., Vereecke, L., De Greve, H., et al. (2015). Structural and adhesive properties of the long polar fimbriae protein LpfD from adherent-invasive Escherichia coli. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 71(8), 1615–1626.
Vancouver
1.
Coppens F, Iyyathurai J, Ruer S, Fioravanti A, Taganna J, Vereecke L, et al. Structural and adhesive properties of the long polar fimbriae protein LpfD from adherent-invasive Escherichia coli. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY. 2015;71(8):1615–26.
MLA
Coppens, Fanny, Jegan Iyyathurai, Segolène Ruer, et al. “Structural and Adhesive Properties of the Long Polar Fimbriae Protein LpfD from Adherent-invasive Escherichia Coli.” ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY 71.8 (2015): 1615–1626. Print.
@article{7064464,
  abstract     = {Crohn's disease (CD) is an inflammatory bowel disease characterized by an exaggerated immune response to commensal microbiota in the intestines of patients. Metagenomic studies have identified specific bacterial species and strains with increased prevalence in CD patients, amongst which is the adherent-invasive Escherichia coli (AIEC) strain LF82. AIEC strains express long polar fimbriae (LPF), which are known to target Peyer's patches in a mouse CD model. Here, the recombinant production of a soluble, self-complemented construct of the LpfD protein of E. coli LF82 is reported and it is demonstrated that it forms the adhesive tip subunit of LPF. The LpfD crystal reveals an N-terminal adhesin domain and a C-terminal pilin domain that connects the adhesin to the minor pilus subunit LpfE. Surface topology and sequence conservation in the adhesin domain hint at a putative receptor-binding pocket as found in the Klebsiella pneumoniae MrkD and E. coli F17-G (GafD) adhesins. Immunohistostaining of murine intestinal tissue sections revealed that LpfD specifically binds to the intestinal mucosa and submucosa. LpfD binding was found to be resistant to treatment with O- or N-glycosidases, but was lost in collagenase-treated tissue sections, indicating the possible involvement of an intestinal matrix-associated protein as the LpfD receptor. LpfD strongly adhered to isolated fibronectin in an in vitro assay, and showed lower levels of binding to collagen V and laminin and no binding to collagens I, III and IV.},
  author       = {Coppens, Fanny and Iyyathurai, Jegan and Ruer, Segol{\`e}ne and Fioravanti, Antonella and Taganna, Joemar and Vereecke, Lars and De Greve, Henri and Remaut, Han},
  issn         = {1399-0047},
  journal      = {ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY},
  language     = {eng},
  number       = {8},
  pages        = {1615--1626},
  title        = {Structural and adhesive properties of the long polar fimbriae protein LpfD from adherent-invasive Escherichia coli},
  url          = {http://dx.doi.org/10.1107/S1399004715009803},
  volume       = {71},
  year         = {2015},
}

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