g(m3)-ganglioside and Chancroid

g(m3)-ganglioside has been researched along with Chancroid* in 1 studies

Other Studies

1 other study(ies) available for g(m3)-ganglioside and Chancroid

Article	Year
Binding of Haemophilus ducreyi to carbohydrate receptors is mediated by the 58.5-kDa GroEL heat shock protein. Microbes and infection, 2006, Volume: 8, Issue:9-10 The bacterium Haemophilus ducreyi causes the sexually transmitted disease chancroid, which is characterized by the appearance of mucocutaneous, persistent ulcers on the external genitals. To identify carbohydrate receptors that mediate the attachment of this pathogen to host cells, we investigated the binding of 35S-methionine-labeled H. ducreyi strains to a panel of defined glycosphingolipids that were separated on thin layer chromatography plates. H. ducreyi bound to lactosylceramide, gangliotriaosylceramide, gangliotetraosylceramide, neolactotetraosylceramide, the GM3 ganglioside, and sulfatide. To elucidate the role of the surface-located 58.5-kDa GroEL heat shock protein (HSP) of H. ducreyi in attachment, we investigated the binding of purified HSP to the same panel of glycosphingolipids. Our results suggest that the 58.5-kDa GroEL HSP of H. ducreyi is responsible for the attachment of this bacterium to the majority of the tested glycosphingolipids, and thus represents a potential bacterial adhesin. Topics: Attachment Sites, Microbiological; Binding Sites; Carbohydrate Sequence; Chancroid; Chaperonin 60; Chromatography, Thin Layer; G(M3) Ganglioside; Glycosphingolipids; Haemophilus ducreyi; Humans; Molecular Sequence Data; Sulfoglycosphingolipids	2006

Article

Year

Binding of Haemophilus ducreyi to carbohydrate receptors is mediated by the 58.5-kDa GroEL heat shock protein.

Microbes and infection, 2006, Volume: 8, Issue:9-10

The bacterium Haemophilus ducreyi causes the sexually transmitted disease chancroid, which is characterized by the appearance of mucocutaneous, persistent ulcers on the external genitals. To identify carbohydrate receptors that mediate the attachment of this pathogen to host cells, we investigated the binding of 35S-methionine-labeled H. ducreyi strains to a panel of defined glycosphingolipids that were separated on thin layer chromatography plates. H. ducreyi bound to lactosylceramide, gangliotriaosylceramide, gangliotetraosylceramide, neolactotetraosylceramide, the GM3 ganglioside, and sulfatide. To elucidate the role of the surface-located 58.5-kDa GroEL heat shock protein (HSP) of H. ducreyi in attachment, we investigated the binding of purified HSP to the same panel of glycosphingolipids. Our results suggest that the 58.5-kDa GroEL HSP of H. ducreyi is responsible for the attachment of this bacterium to the majority of the tested glycosphingolipids, and thus represents a potential bacterial adhesin.

Topics: Attachment Sites, Microbiological; Binding Sites; Carbohydrate Sequence; Chancroid; Chaperonin 60; Chromatography, Thin Layer; G(M3) Ganglioside; Glycosphingolipids; Haemophilus ducreyi; Humans; Molecular Sequence Data; Sulfoglycosphingolipids

2006