Characterization of a reverse gyrase from the extremely thermophilic hydrogen-oxidizing eubacterium Calderobacterium hydrogenophilum |
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| Authors: | Ladislav Andera Karel Mikulik Nadja D. Savelyeva |
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| Affiliation: | Membrane Glycobiology Group, Department of Medical Biochemistry, University of Gothenburg, Gothenburg, Sweden; Department of Molecular Microbiology, Faculty of Biology, Vrije Universiteit, Amsterdam, The Netherlands |
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| Abstract: | Abstract Non-acid and acid glycolipids were isolated from the small intestine of a newborn calf and tested for the ability to bind Escherichia coli carrying K99 fimbriae. The bacteria did not bind to any of the non-acid glycolipids, whereas in the acid glycolipid fraction several gangliosides were detected which bind to K99 fimbriae. Gangliosides capable of binding K99 fimbriated E. coli were characterized as NeuGc-GM3, NeuGc-GM2, NeuGc-GD1a NeuAc-SPG and NeuAc-SPG. No binding was detected to NeuAc-GM3 and NeuGc-GM1. |
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| Keywords: | K99 Fimbriae Receptor Ganglioside Calf Small intestine Escherichia coli |
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