Novel cell‐binding activity specific for <i>N</i>‐acetyl‐D‐glucosamine in an <i>Escherichia coli</i> strain

Väisänen‐Rhen, Vuokko; Korhonen, Timo; Finne, Jukka

doi:10.1016/0014-5793(83)80453-0

Cited by 39 publications

(30 citation statements)

References 17 publications

(6 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…A human pyelonephritogenic E. coli isolate possessing a related adhesion phenotype has also been documented (39). The fimbriae of this strain, which is responsible for glucosamine-sensitive hemagglutination of endo-␤-galactosidase-treated human erythrocytes, have been termed G fimbriae (32,39). As reported here, we have identified the lectin protein gene gafD of E. coli G fimbriae, expressed the gene, isolated the gene product, and established the receptor-binding ability of the isolated lectin protein.…”

mentioning

confidence: 72%

“…G-fimbriated bacteria agglutinate erythrocytes rich in terminal N-acetyl-D-glucosamine residues (32). GlcNAc is readily exposed on erythrocytes treated with endo-␤-galactosidase (39). Receptor binding was therefore assayed by agglutination of endo-␤-galactosidase-treated human erythrocytes in bacterial suspensions.…”

Section: Resultsmentioning

confidence: 99%

“…Autoagglutination is seen when G-fimbriated bacteria are mixed in a buffer on a glass slide; the bacteria strongly agglutinate without the addition of any antibodies. G-fimbriated bacteria also agglutinate endo-␤-galactosidase-treated human erythrocytes (39). Autoagglutination and hemagglutination are both inhibited in the presence of N-acetyl-D-glucosamine (32), suggesting that G fimbriae bind to a common receptor structure present on both cell types.…”

Section: Discussionmentioning

confidence: 99%

“…A wide variety of host structures may function as receptors for fimbriae (5,9,17,32,39). Yet, the receptor specificity of individual fimbrial lectin proteins is comparable to that of plant lectins or antibodies.…”

mentioning

confidence: 99%

“…Bacteria expressing these fimbriae adhere to intestinal brush borders, and this attachment can be inhibited with Nacetyl-D-glucosamine (23,24). A human pyelonephritogenic E. coli isolate possessing a related adhesion phenotype has also been documented (39). The fimbriae of this strain, which is responsible for glucosamine-sensitive hemagglutination of endo-␤-galactosidase-treated human erythrocytes, have been termed G fimbriae (32,39).…”

mentioning

confidence: 99%

See 4 more Smart Citations

The Escherichia coli G-fimbrial lectin protein participates both in fimbrial biogenesis and in recognition of the receptor N-acetyl-D-glucosamine

et al. 1995

View full text Add to dashboard Cite

The gafD gene encoding the N-acetyl-D-glucosamine-specific fimbrial lectin (adhesin) protein GafD of uropathogenic Escherichia coli was cloned and subjected to genetic analysis. The corresponding gene product was isolated as a MalE fusion protein. The lectin gene was identified with the aid of deletion mutagenesis; mutations in gafD impaired either receptor binding or both receptor binding and fimbria production, depending on the mutation created. All mutants converted to wild-type expressors when complemented in trans with the cloned intact gafD gene. The predicted 354-amino-acid sequence of GafD, deduced from the nucleotide sequence, is closely related to those of the fimbria-associated F17-G and F17b-G proteins coded for by enterotoxigenic and invasive E. coli strains. Isolated GafD was shown to recognize N-acetyl-D-glucosamine by virtue of specific binding to an immobilized receptor, thus proving directly that GafD is a sugar-binding protein. Our results indicate that GafD as such is sufficient for receptor recognition and that the protein also participates in fimbrial biogenesis.Colonization of host epithelial cell surfaces is a prerequisite for many bacterial infections (5, 9, 17). Such colonization is promoted by bacterial adherence to receptor structures present on host epithelial surfaces. Among enteric bacteria, binding to host receptors is often mediated by adhesion organelles called fimbriae or pili (5, 9, 17) expressed on the bacterial cell surface.Fimbriae are filamentous polymers of protein subunits called fimbrillins (5, 9). P fimbriae of uropathogenic Escherichia coli strains (10, 31, 33) as well as S (8, 30, 37) and the common type 1 fimbriae (1, 17) possess a receptor-binding molecular organelle attached to the fimbrial filament. This

show abstract

mentioning

confidence: 72%

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations