Elucidating the glycan-binding specificity and structure of Cucumis melo agglutinin, a new R-type lectin

• Jon Lundstrøm,
• Emilie Gillon,
• Valérie Chazalet,
• Nicole Kerekes,
• Antonio Di Maio,
• Ten Feizi,
• Yan Liu,
• Annabelle Varrot and
• Daniel Bojar

Beilstein J. Org. Chem. 2024, 20, 306–320, doi:10.3762/bjoc.20.31

• garnered attention for their roles as laboratory probes and potential therapeutics. Here, we report the discovery and characterization of Cucumis melo agglutinin (CMA1), a new R-type lectin from melon. Our findings reveal CMA1’s unique glycan-binding profile, mechanistically explained by its 3D structure

• , augmenting our understanding of R-type lectins. We expressed CMA1 recombinantly and assessed its binding specificity using multiple glycan arrays, covering 1,046 unique sequences. This resulted in a complex binding profile, strongly preferring C2-substituted, beta-linked galactose (both GalNAc and Fuca1-2Gal

• ), which we contrasted with the established R-type lectin Ricinus communis agglutinin 1 (RCA1). We also report binding of specific glycosaminoglycan subtypes and a general enhancement of binding by sulfation. Further validation using agglutination, thermal shift assays, and surface plasmon resonance

Decarboxylative 1,3-dipolar cycloaddition of amino acids for the synthesis of heterocyclic compounds

• Xiaofeng Zhang,
• Xiaoming Ma and
• Wei Zhang

Beilstein J. Org. Chem. 2023, 19, 1677–1693, doi:10.3762/bjoc.19.123

• aldehydes and α-amino esters (via dehydration) or α-amino acids (via decarboxylation) could be classified based on the substitution groups on the N atom to: 1) N-substituted (N–R type), 2) hydrogen containing (N–H type), and 3) metal complexes (N–M type) (Figure 1) [16][17]. These AMYs could also be

• ][26][27][28]. It is worth noting that among the products 1a–d, only compound 1d has hydrogen atoms on both the nitrogen and α-carbon atoms, which makes it suitable to be used for a second cycloaddition to form double [3 + 2] cycloaddition products 2 [29][30]. The N–R-type AMYs B1 and B2 bearing an Ar

• stereoselectivity which limits the synthetic utility of non-stabilized AMYs of type C. There are over 300 papers on the amino acid-based decarboxylative [3 + 2] cycloadditions of N–R-type AMYs B1 (such as that derived from proline) and B2 [31][32][33][34][35][36][37][38][39][40][41][42][43][44][45][46][47][48][49

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

• (MSHA), C-type lectins, and R-type lectins. Furthermore, the filamentous hemagglutinin (FHA) and the heparin-binding hemagglutinin (HBHA) as glycosaminoglycan-binding protein families are also discussed (Table 3, Figure 4). Agglutinin-like sequences Based on bioinformatic analysis, the two Mtb gene

• africum, which is currently limited to West Africa [94]. Thus, the potential C-type lectin of Mtb might not be essential for a typical TB infection in humans. However, cell localization and function need to be investigated in further detail. R-Type lectin R-Type lectins are classified as lectins

• containing a carbohydrate-recognition domain similar to the CRD in ricin, a toxin of the poisonous plant Ricinus communis. R-type lectins have been detected in plants, animals, and bacteria. Plant R-type lectins often contain a separate subunit functioning as a toxin. Furthermore, ricin-type lectin domains