The Escherichia coli G-fimbrial lectin protein participates both in fimbrial biogenesis and in recognition of the receptor N-acetyl-D-glucosamine
| Autor: | Mikael Rhen, Suvi Taira, A Makkonen, Eeva-Liisa Nurmiaho-Lassila, Sirkku Saarela |
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| Rok vydání: | 1995 |
| Předmět: |
Recombinant Fusion Proteins
DNA Mutational Analysis Molecular Sequence Data Restriction Mapping Mutant Receptors Cell Surface Biology medicine.disease_cause Microbiology Bacterial Adhesion Acetylglucosamine Gene product 03 medical and health sciences Lectins Escherichia coli Morphogenesis medicine Amino Acid Sequence Molecular Biology Peptide sequence 030304 developmental biology 0303 health sciences Mutation Base Sequence Sequence Homology Amino Acid 030306 microbiology Nucleic acid sequence Hemagglutination Tests Sequence Analysis DNA Molecular biology Fusion protein Bacterial adhesin Microscopy Electron Genes Bacterial Fimbriae Bacterial Research Article |
| Zdroj: | Journal of Bacteriology. 177:1477-1484 |
| ISSN: | 1098-5530 0021-9193 |
| DOI: | 10.1128/jb.177.6.1477-1484.1995 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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