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

Journal article
Authors Martina Pantzar
Susann Teneberg
Teresa Lagergård
Published in Microbes and infection / Institut Pasteur
Volume 8
Issue 9-10
Pages 2452-8
ISSN 1286-4579
Publication year 2006
Published at Institute of Biomedicine, Department of Microbiology and Immunology
Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology
Pages 2452-8
Language en
Keywords Attachment Sites, Microbiological, physiology, Binding Sites, Carbohydrate Sequence, Chancroid, microbiology, Chromatography, Thin Layer, methods, G(M3) Ganglioside, chemistry, metabolism, Glycosphingolipids, chemistry, isolation & purification, metabolism, GroEL Protein, metabolism, Haemophilus ducreyi, isolation & purification, metabolism, Humans, Molecular Sequence Data, Sulfoglycosphingolipids, chemistry, metabolism
Subject categories Medical and Health Sciences


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.

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