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

• ). In this paper we review previous studies on the carbohydrate-binding characteristics of mycobacteria and related Mtb proteins, discussing their potential relevance to Mtb infection and pathogenesis. Keywords: adhesion; carbohydrates; fimbriae; lectins; Mycobacterium tuberculosis; pili; Introduction

• bacteria, which is crucial for the formation of well-organized superstructures such as biofilms. In contrast to eukaryotic lectins, bacterial lectins commonly occur in the form of filamentous protein appendages projecting from their surface, known as fimbriae and pili [63]. Fimbriae are present in high

• bacterial lectins are the mannose-specific FimH of type 1 fimbriae and the galabiose-specific PapG of P fimbriae, expressed by Enterobactericea, such as Escherichia coli (E. coli). While type 1-fimbrial expression of E. coli is associated with urinary tract infections, the presence of P fimbriae is

Non-native autoinducer analogs capable of modulating the SdiA quorum sensing receptor in Salmonella enterica serovar Typhimurium

• Matthew J. Styles and
• Helen E. Blackwell

Beilstein J. Org. Chem. 2018, 14, 2651–2664, doi:10.3762/bjoc.14.243

• . Typhimurium responds to exogenously supplied natural AHLs, AHL-dependent SdiA regulons were identified in both S. Typhimurium [27][28] and E. coli [14][29][30][31]. In S. Typhimurium, SdiA promotes transcription of pefI, srgA-E, and rck [28][32]. pefI and srgA are members of the plasmid encoded fimbriae (pef

Diazirine-functionalized mannosides for photoaffinity labeling: trouble with FimH

• Femke Beiroth,
• Tomas Koudelka,
• Thorsten Overath,
• Stefan D. Knight,
• Andreas Tholey and
• Thisbe K. Lindhorst

Beilstein J. Org. Chem. 2018, 14, 1890–1900, doi:10.3762/bjoc.14.163

• with optimized photolabeling conditions and high-end mass spectrometry. Results and Discussion FimH is a fimbrial lectin found at the tips of adhesive organelles (type 1 fimbriae), which are projecting from the surface of enterobacteriaceae such as E. coli. Fimbriae mediate firm attachment (adhesion

What contributes to an effective mannose recognition domain?

• Christoph P. Sager,
• Deniz Eriş,
• Martin Smieško,
• Rachel Hevey and
• Beat Ernst

Beilstein J. Org. Chem. 2017, 13, 2584–2595, doi:10.3762/bjoc.13.255

• to 1.7 nM for glycosylated gp120 (25 glycosylation sites) [43][77]. In the case of UPEC, each bacterium contains three to five hundred fimbriae to potentiate multivalency, as each FimHLD (I) at the fimbrial tip can interact with mammalian UPIa [78]. Multivalent glycosides have also been investigated

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

• control of carbohydrate-specific bacterial adhesion, it has become our goal to synthesise azobenzene mannosides as photoswitchable inhibitors of type 1 fimbriae-mediated adhesion of E. coli. An azobenzene mannobioside 2 was prepared and its photochromic properties were investigated. The E→Z isomerisation

• powerful antagonists is highly desirable, however, ideally on demand, that is, in a specific and spatially as well as temporally resolved way. Often bacterial adhesion depends on the interaction of adhesive organelles called fimbriae. They project from the surface of bacteria and contain lectin domains to

• the scope of carbohydrate-based antiadhesives, it has become our goal to make photoswitchable ligands of bacterial lectins to allow blocking of bacterial adhesion in a photocontrolled manner. One of the best-known fimbriae are the type 1 fimbriae of uropathogenic E. coli (UPEC), which comprise the α-D

Synthetic glycopeptides and glycoproteins with applications in biological research

• Ulrika Westerlind

Beilstein J. Org. Chem. 2012, 8, 804–818, doi:10.3762/bjoc.8.90

• monosaccharide ligands have been prepared and evaluated [123]. The type 1 fimbriated Echerichia coli is a pathogen responsible for urinary tract infections with millions of cases every year [124]. The type 1 fimbriae have been identified to be a major contributor to these infections [125][126]. The FimH lectin

• on type 1 fimbriae is an attractive target for the inhibition of α-mannose-mediated cell adhesion [127][128][129][130][131]. Previous X-ray studies have proven that the FimH lectin has a monovalent binding site recognizing α-D-mannose [132][133]. In close proximity to the mannose-binding crevice, two

En route to photoaffinity labeling of the bacterial lectin FimH

• Thisbe K. Lindhorst,
• Michaela Märten,
• Andreas Fuchs and
• Stefan D. Knight

Beilstein J. Org. Chem. 2010, 6, 810–822, doi:10.3762/bjoc.6.91

• ) [1]. It has become our goal to utilize this methodology for the investigation of carbohydrate binding of the bacterial lectin FimH. The protein FimH is found on the tips of type 1 fimbriae, long adhesive filamentous appendages on the surface of many bacteria, such as Escherichia coli [2][3][4][5]. In

• -mannoside (pNPMan), respectively (Table 1). When these mannosides were tested as inhibitors of type 1 fimbriae-mediated bacterial adhesion to a mannan-coated surface in an ELISA [21][22], IC50-values were obtained, which reflect the concentration of the derivative employed, that leads to 50% inhibition of

A bivalent glycopeptide to target two putative carbohydrate binding sites on FimH

• Thisbe K. Lindhorst,
• Kathrin Bruegge,
• Andreas Fuchs and
• Oliver Sperling

Beilstein J. Org. Chem. 2010, 6, 801–809, doi:10.3762/bjoc.6.90

• 1 fimbriae with a monovalent carbohydrate recognition domain (CRD) that is known from X-ray studies. However, binding studies with multivalent ligands have suggested an additional carbohydrate-binding site on this protein. In order to prove this hypothesis, a bivalent glycopeptide ligand with the

• persistent biofilms. In all cases of bacterial adhesion and of biofilm formation severe health problems can result for the host organism [1][2]. A number of microbial adhesins are known, that co-operate in the adhesion process [3], such as the fimbriae, which are long filamentous adhesive organells on the

• surface of many bacteria, comprising carbohydrate-binding sub-units [4][5][6]. The type 1 fimbriae, for example, which are widely spread among the Enterobacteriaceae are terminated with the mannose-specific protein FimH. FimH is structured in the form of two domains, a carbohydrate-specific adhesin domain