Lectins of Mycobacterium tuberculosis – rarely studied proteins

• Katharina Kolbe,
• Sri Kumar Veleti,
• Norbert Reiling and
• Thisbe K. Lindhorst

Beilstein J. Org. Chem. 2019, 15, 1–15, doi:10.3762/bjoc.15.1

• , which act as FimH antagonists, for example, have been successfully used to significantly reduce the severity of E. coli infections of the urinary tract in mice [66]. Furthermore, preliminary clinical trials with D-mannose indicate promising effects of this monosaccharide on controlling urinary tract

Are D-manno-configured Amadori products ligands of the bacterial lectin FimH?

• Tobias-Elias Gloe,
• Insa Stamer,
• Cornelia Hojnik,
• Tanja M. Wrodnigg and
• Thisbe K. Lindhorst

Beilstein J. Org. Chem. 2015, 11, 1096–1104, doi:10.3762/bjoc.11.123

• glycosylated surface of host cells is a key step in infections caused by type 1-fimbriated bacteria, FimH antagonists that inhibit bacterial adhesion can be valuable for treatment of infectious diseases [7][8]. The structure of type 1-fimbrial lectin FimH has been elucidated in X-ray analysis [9][10][11

Synthesis and testing of the first azobenzene mannobioside as photoswitchable ligand for the bacterial lectin FimH

• Vijayanand Chandrasekaran,
• Katharina Kolbe,
• Femke Beiroth and
• Thisbe K. Lindhorst

Beilstein J. Org. Chem. 2013, 9, 223–233, doi:10.3762/bjoc.9.26

• adhesive surfaces. Keywords: azobenzene glycosides; bacterial adhesion; E/Z photoisomerisation; FimH antagonists; mannobiosides; molecular switches; sweet switches; Introduction Adhesion of bacteria to surfaces can be a severe problem both in vivo and in vitro. Hence, inhibition of bacterial adhesion by

• -mannosyl-specific lectin FimH at the tip of the fimbrial shaft. FimH antagonists are currently considered as new therapeutics for the treatment of urinary tract infections [6]. The carbohydrate specificity of FimH has been investigated in great detail [7] and its structure is well-known from several X-ray

• introduced lately and shown to be of medical relevance as FimH antagonists [6]. Thus, our novel “sweet switches” [15] appear to be highly promising FimH ligands, with the additional feature of a photoswitchable moiety. The biomedicinal potential of azobenzene glycosides seems even higher when their