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Binding of Actinomyces naeslundii to glycosphingolipids
- Publication Year :
- 1987
-
Abstract
- The type 2 fimbrial lectin of Actinomyces naeslundii WVU45 mediated the binding of this bacterium to glycosphingolipids chromatographed on thin-layer silica gel plates. Radioiodinated bacteria attached to GM1, GD1b, and globoside. After chromatograms were treated with sialidase, the bacteria also bound to GD1a and GT1b. The actinomyces lectin apparently recognized the Gal beta 3GalNAc termini of these gangliosides and the GalNAc beta 3Gal terminus of globoside, suggesting that glycolipids containing these sequences may serve as receptors for A. naeslundii on mammalian cells.
- Subjects :
- biology
Globoside
Globosides
Immunology
Lectin
biology.organism_classification
Sialidase
Microbiology
Glycosphingolipids
carbohydrates (lipids)
Infectious Diseases
Glycolipid
Biochemistry
Gangliosides
Lectins
Actinomyces naeslundii
biology.protein
Actinomyces
Parasitology
lipids (amino acids, peptides, and proteins)
Chromatography, Thin Layer
Receptor
Bacteria
Research Article
Subjects
Details
- Language :
- English
- Database :
- OpenAIRE
- Accession number :
- edsair.doi.dedup.....bb984a918118c19ad5745ce3a3deede1