Lectin-binding characteristics of a Lyme borreliosis spirochete Borrelia burgdorferi sensu stricto
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
16295662
DOI
10.1007/bf02931571
Knihovny.cz E-zdroje
- MeSH
- Borrelia burgdorferi metabolismus patogenita ultrastruktura MeSH
- buněčná membrána metabolismus ultrastruktura MeSH
- elektronová kryomikroskopie MeSH
- glykokonjugáty chemie metabolismus MeSH
- králíci MeSH
- lektiny metabolismus MeSH
- lidé MeSH
- lymeská nemoc mikrobiologie MeSH
- techniky in vitro MeSH
- zvířata MeSH
- Check Tag
- králíci MeSH
- lidé MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- glykokonjugáty MeSH
- lektiny MeSH
Borrelial glycoconjugates were localized by labeled lectins on ultrathin cryosections and on surfaces of intact negatively stained bacteria. Protein-saccharide complexes in these glycoconjugates were partially characterized by means of enzyme deglycosylation and mild alkali pretreatment of cryosections. The results of labeling were examined by transmission electron microscopy. Statistically evaluated results (relative labeling index, chi2 test) of gold labeling indicated that surfaces of Borrelia burgdorferi strain B31 and external (outer) membrane vesicles (MVs) were covered with glycoconjugates containing O-glycosidically linked N-acetyl-D-galactosamine (GalNAc) and N-glycosidically linked N-acetyl-D-glucosamine (GlcNAc). The presence of N-linked GalNAc, sialic acid, mannose and fucose on the surfaces of outer membranes and MVs was probably due to an adherence of BSK-H medium components, especially rabbit serum, to Borrelia surfaces.
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