An Attempt to Identify the Intestinal Receptor for the K88 Adhesin by Means of a Haemagglutination Inhibition Test using Glycoproteins and Fractions from Sow Colostrum

Gibbons, R. A.; Jones, G. W.; Sellwood, R.

doi:10.1099/00221287-86-2-228

Cited by 80 publications

(49 citation statements)

References 41 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Furthermore, the abolition of the response seen with these sugars suggests that binding to the mucosa is a specific, receptor-mediated reaction in which the mucosal immunogens bind to specific glycoproteins or glycolipids on the villous epithelium . In this respect, intestinal uptake of these antigens differs significantly from the antigen sampling mechanism suggested for the uptake of orally administered antigens (7,8,10,11,25).…”

Section: Discussionmentioning

confidence: 76%

“…The surface antigens that confer adhesive properties to a number of strains of enterotoxigenic E. coli (ETEC) have been identified as nonflagellar, filamentous proteinaceous appendages, called fimbrae or pili (9) . Examples include the CFA I and CFA II pili of human ETEC strains and the K88, K99, F41 and 987P pili of animal ETEC strains (10)(11)(12)(13)(14) . In addition, we have examined the ability of a number of other proteins that have no apparent role in colonization to prime the immune system upon oral feeding.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Oral vaccination. Identification of classes of proteins that provoke an immune response upon oral feeding.

Aizpurua¹,

Russell-Jones²

1988

The Journal of Experimental Medicine

203

View full text Add to dashboard Cite

Oral immunization of an animal is generally hard to achieve unless large quantities of antigen are administered. In this study a number of antigens were tested for their ability to elicit a systemic immune response upon oral administration. It was found that bacterial pili, LTB, lectins, and a viral hemagglutinin were all able to elicit significant antibody titers upon oral feeding. The immune response thus generated to LTB and K99 pili could be completely abolished by cofeeding a number of sugars that have close structural homology to the terminal sugars of the GM1 and GM2 gangliosides to which these molecules are known to bind. All of the proteins that were active in oral immunization are known to possess "lectin or lectin-like" binding activities. It is therefore proposed that these molecules are able to bind to glycolipids and glycoproteins on the intestinal mucosa and to stimulate these cells to transport the proteins into the systemic circulation, thereby eliciting a systemic immune response. Molecules that did not possess this binding activity were unable to elicit significant responses at the doses tested.

show abstract

Section: Discussionmentioning

confidence: 76%

mentioning

confidence: 99%

Oral vaccination. Identification of classes of proteins that provoke an immune response upon oral feeding.

Aizpurua¹,

Russell-Jones²

1988

The Journal of Experimental Medicine

203

View full text Add to dashboard Cite

show abstract

“…The K88 antigen agglutinates guinea-pig red cells (Stirm et al, 1967;Jones and Rutter, 1974), and attempts to study the chemical aspects of adhesion by means of this reaction have been reported (Gibbons, Jones and Sellwood, 1975). It would have been preferable to use a natural intestinal receptor, but the technique involving adhesion of E. coli to disks of intestinal tissue (Jones and Rutter, 1972) is laborious.…”

mentioning

confidence: 99%

Adhesion of Enteropathogenic Escherichia Coli to Pig Intestinal Brush Borders: The Existence of Two Pig Phenotypes

Sellwood

Gibbons

Jones

et al. 1975

Journal of Medical Microbiology

Self Cite

281

190

View full text Add to dashboard Cite

PLATES XXVIII AND XXIX NEONATAL diarrhoea in piglets follows the proliferation of certain strains of Escherichia coli in the small intestine (Smith and Jones, 1963). These enteropathogenic strains synthesise enterotoxins which produce diarrhoea and dehydration that frequently result in the death of the piglets (Kohler, 1968;Smith and Gyles, 1970;Smith and Linggood, 1971). The rapid proliferation of E. coli in the small intestine appears to be attributable to the ability of the bacteria to attach themselves to the intestinal epithelium (Arbuckle, 1970; Drees and Wader, 1970a and b; Bertschinger, Moon and Whipp, 1972) and thereby avoid removal from the small intestine by peristalsis (Dixon, 1960). Sojka (1965) noted that the majority of E. coli strains isolated from cases of neonatal piglet diarrhoea possess a surface antigen designated K88, and it has been shown that this antigen is an essential virulence determinant (Smith and Linggood, 1971 ;Jones and Rutter, 1972) apparently because it enabled K88-positive E. coli to attach to the intestinal lining (Jones and Rutter, 1972).To investigate the interaction between the host mucosal surface and K88-positive E. coli a convenient test system is essential. The K88 antigen agglutinates guinea-pig red cells (Stirm et al., 1967;Jones and Rutter, 1974), and attempts to study the chemical aspects of adhesion by means of this reaction have been reported (Gibbons, Jones and Sellwood, 1975). It would have been preferable to use a natural intestinal receptor, but the technique involving adhesion of E. coli to disks of intestinal tissue (Jones and Rutter, 1972) is laborious. This paper describes a simple in-vitro technique that demonstrates adhesion of K88-positive E. coli to brush borders from pig intestinal cells; a survey of pigs in respect of the ability of their brush borders to adhere to E. coli is also described. MATERIALS AND METHODS

show abstract

“…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 intestinal epithelial cells (4,11,12,17,19,37,39,51,58). It has been clearly demonstrated that all three K88 adhesin variants are lectins and that they recognize carbohydrate structures expressed on host cell glycoconjugates.…”

mentioning

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

View full text Add to dashboard Cite

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...

show abstract

An Attempt to Identify the Intestinal Receptor for the K88 Adhesin by Means of a Haemagglutination Inhibition Test using Glycoproteins and Fractions from Sow Colostrum

Cited by 80 publications

References 41 publications

Oral vaccination. Identification of classes of proteins that provoke an immune response upon oral feeding.

Oral vaccination. Identification of classes of proteins that provoke an immune response upon oral feeding.

Adhesion of Enteropathogenic Escherichia Coli to Pig Intestinal Brush Borders: The Existence of Two Pig Phenotypes

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

Contact Info

Product

Resources

About