| Literature DB >> 3804448 |
M J Brennan, R A Joralmon, J O Cisar, A L Sandberg.
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.Entities:
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Year: 1987 PMID: 3804448 PMCID: PMC260356 DOI: 10.1128/iai.55.2.487-489.1987
Source DB: PubMed Journal: Infect Immun ISSN: 0019-9567 Impact factor: 3.441