K ANTIGENS K88ab(L) AND K88ac(L) IN <i>E. coli</i>

Ørskov, Ida; Ørskov, Frits; Sojka, W.J.; Wittig, W

doi:10.1111/apm.1964.62.3.439

Cited by 117 publications

(42 citation statements)

References 5 publications

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“…Three serologically distinguishable variants of K88 adhesin (K88ab, K88ac, and K88ad) have been identified (21,40). Each variant consists of a conserved antigenic region shared by all three variants, designated a, and variant-specific antigenic regions, designated b, c, and d for K88ab, K88ac, and K88ad, respectively (13,29).…”

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confidence: 99%

Evaluation of Receptor Binding Specificity ofEscherichia coliK88 (F4) Fimbrial Adhesin Variants Using Porcine Serum Transferrin and Glycosphingolipids as Model Receptors

Grange

Mouricout²,

Levery

et al. 2002

Infect Immun

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Diarrheal disease caused by enterotoxigenic Escherichia coli expressing the K88 (F4) fimbrial adhesin (K88 ETEC) is a significant source of mortality and morbidity among newborn and weaned piglets. K88 fimbrial adhesins are filamentous surface appendages whose lectin (carbohydrate-binding) activity allows K88 ETEC to attach to specific glycoconjugates (receptors) on porcine intestinal epithelial cells. There are three variants of K88 adhesin (K88ab, K88ac, and K88ad), which possess different, yet related, carbohydrate-binding specificities. We used porcine serum transferrin (pSTf) and purified glycosphingolipids (GSL) to begin to define the minimal recognition sequence for K88 adhesin variants. We found that K88ab adhesin binds with high affinity to pSTf (dissociation constant, 75 M), while neither K88ac nor K88ad adhesin recognizes pSTf. Degradation of the N-glycan on pSTf by extensive metaperiodate treatment abolished its interaction with the K88ab adhesin, indicating that the K88ab adhesin binds to the single N-glycan found on pSTf. Using exoglycosidase digestion of the pSTf glycan, we demonstrated that K88ab adhesin recognizes N-acetylglucosamine (GlcNAc) residues in the core of the N-glycan on pSTf. All three K88 variants were found to bind preferentially to GSL containing a ␤-linked N-acetylhexosamine (HexNAc), either GlcNAc or N-acetylgalactosamine, in the terminal position or, alternatively, in the penultimate position with galactose in the terminal position. Considering the results from pSTf and GSL binding studies together, we propose that the minimal recognition sequence for the K88 adhesin variants contains a ␤-linked HexNAc. In addition, the presence of a terminal galactose ␤-linked to this HexNAc residue enhances K88 adhesin binding.Diarrheal disease caused by enterotoxigenic Escherichia coli expressing the K88 (F4) fimbrial adhesin (K88 ETEC) is a significant source of mortality and morbidity among newborn and weaned piglets (9,25,38,41,59). K88 fimbrial adhesins are filamentous surface appendages whose lectin (carbohydratebinding) activity allows K88 ETEC to attach to specific glycoconjugates (receptors) on porcine intestinal epithelial cells (28). Attachment of bacteria to their receptors on intestinal epithelial cells is an essential step in the colonization of the small intestine by ETEC.Three serologically distinguishable variants of K88 adhesin (K88ab, K88ac, and K88ad) have been identified (21, 40). Each variant consists of a conserved antigenic region shared by all three variants, designated a, and variant-specific antigenic regions, designated b, c, and d for K88ab, K88ac, and K88ad, respectively (13, 29). The antigenic differences among the three K88 variants can be ascribed exclusively to a small number of nucleotide changes in the major fimbrial subunit gene, resulting in the amino acid substitutions that distinguish the three K88 variants. Several researchers have investigated the molecular interaction of K88 fimbrial adhesin variants with erythrocytes, intestinal mucus, and intestina...

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confidence: 99%

Evaluation of Receptor Binding Specificity ofEscherichia coliK88 (F4) Fimbrial Adhesin Variants Using Porcine Serum Transferrin and Glycosphingolipids as Model Receptors

Grange

Mouricout²,

Levery

et al. 2002

Infect Immun

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“…FaeG Employs a Variable Domain to Diversify Receptor Recognition-Apart from the ad isotype crystallized in complex with lactose (see above), two additional FaeG serotypes are known (ab and ac) that differ in receptor binding profile (17,18). Co-crystallization of donor strand complemented FaeG ab and FaeG ac in the presence of a selection of previously identified carbohydrate ligands (galactose, lactose, globotriaose (Gal␣1-4Gal␤1-4Glc), galabiose (Gal␣1-4Gal), N-acetyl galactosamine) (30) did not result in the x-ray structures of the binding complexes.…”

Section: Structural Insight Into Receptor Binding By the F4 Fimbrialmentioning

confidence: 99%

“…Therefore, contrary to the most well studied chaperone/usher pili, where receptor binding is determined by a single two-domain adhesin incorporated at the fimbrial tip, binding characteristics of F4 fimbriae are part of the major subunit and are displayed throughout the length of the fiber (15,16). Three naturally occurring serological variants of F4 fimbriae (F4 ab , F4 ac , and F4 ad ) each feature a related but yet different binding and hemagglutination profile (17,18). Differences in binding specificity were attributed to each of the three F4 fimbriae variants (F4 ab , F4 ac , and F4 ad ), and could be interchanged by replacement of a residue stretch in the FaeG protein (19).…”

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confidence: 99%

Structural and Functional Insight into the Carbohydrate Receptor Binding of F4 Fimbriae-producing Enterotoxigenic Escherichia coli

Moonens

Broeck

Kerpel

et al. 2015

Journal of Biological Chemistry

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Background: F4 fimbriae produced by enterotoxigenic Escherichia coli mediate attachment to eukaryotic host receptors. Results: The structure of lactose bound to the F4 fimbrial adhesin FaeG ad was elucidated. Conclusion: Lactose interacts at a subdomain grafted on the FaeG ad core domain. Significance: The co-complex structure explains the finely tuned receptor specificity of F4 ad fimbriae; additionally, the carbohydrate binding site differs among FaeG variants.

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“…At least three different serotypes of K88 fimbriae, K88ab, K88ac and K88ad exist [38,39]. The differences between the K88ab and the K88ac fimbriae were shown to be located in the major subunit FaeG.…”

Section: K88 Fimbriaementioning

confidence: 99%

Molecular and structural aspects of fimbriae biosynthesis and assembly in Escherichia coli

Mol¹

1996

FEMS Microbiology Reviews

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Fimbriae are long filamentous polymeric protein structures located at the surface of bacterial cells. They enable the bacteria to bind to specific receptor structures and thereby to colonise specific surfaces. Fimbriae consist of so-called major and minor subunits, which form, in a specific order, the fimbrial structure. In this review emphasis is put on the genetic organisation, regulation and especially on the biosynthesis of fimbriae of enterotoxigenic Escherichia coli strains, and more in particular on K88 and related fimbriae, with ample reference to the well-studied P and type 1 fimbriae. The biosynthesis of these fimbriae requires two specific and unique proteins, a periplasmic chaperone and an outer membrane located molecular usher ('doorkeeper'). Molecular and structural aspects of the secretion of fimbrial subunits across the cytoplasmic membrane, the interaction of these subunits with the periplasmic molecular chaperone, their translocation to the inner site of the outer membrane and their interaction with the usher protein, as well as the (ordered) translocation of the subunits across the outer membrane and their assembly into a growing fimbrial structure will be described. A model for K88 fimbriae is presented.

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K ANTIGENS K88ab(L) AND K88ac(L) IN E. coli

Cited by 117 publications

References 5 publications

Evaluation of Receptor Binding Specificity ofEscherichia coliK88 (F4) Fimbrial Adhesin Variants Using Porcine Serum Transferrin and Glycosphingolipids as Model Receptors

Evaluation of Receptor Binding Specificity ofEscherichia coliK88 (F4) Fimbrial Adhesin Variants Using Porcine Serum Transferrin and Glycosphingolipids as Model Receptors

Structural and Functional Insight into the Carbohydrate Receptor Binding of F4 Fimbriae-producing Enterotoxigenic Escherichia coli

Molecular and structural aspects of fimbriae biosynthesis and assembly in Escherichia coli

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