7ded | pdb_00007ded

Mevo lectin complex with mannoheptose (Man7)

spinqualitylabelsall models 7ded, resolution 2.23Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7ded is a 7 chain structure with sequence from Methanococcus voltae A3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.228Å Ligands: EDO, MAN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D7DTD6_METV3 Publication Abstract from PubMed Mannose-binding lectins can specifically recognize and bind complex glycan structures on pathogens and have potential as anti-viral and anti-bacterial agents. We previously reported the structure of a lectin from an archaeal species, Mevo lectin, which has specificity towards terminal alpha1,2 linked manno-oligosaccharides. Mycobacterium tuberculosis (M. tuberculosis) expresses mannosylated structures including, lipoarabinomannan (ManLAM) on its surface and exploits C-type lectins to gain entry into the host cells. ManLAM structure has mannose capping with terminal alphaMan(1,2)alphaMan residues and is important for recognition by innate immune cells. Here, we aim to address the specificity of Mevo lectin towards high-mannose type glycans with terminal alphaMan(1,2)alphaMan residues and its effect on M. tuberculosis internalization by macrophages. ITC studies demonstrated that Mevo lectin shows preferential binding towards manno-oligosaccharides with terminal alphaMan(1,2)alphaMan structures, and showed a strong affinity for ManLAM, whereas it binds weakly to Mycobacterium smegmatis (M. smegmatis) lipoarabinomannan (MsmLAM), which displays relatively fewer and shorter mannosyl caps. Crystal structure of Mevo lectin complexed with a Man7D1 revealed the multivalent cross-linking interaction, which explains avidity-based high affinity for these ligands when compared to previously studied manno-oligosaccharides lacking the specific termini. Functional studies suggest that M. tuberculosis internalization by the macrophage was impaired by binding of Mevo lectin to ManLAM present on the surface of M. tuberculosis. Selectivity shown by Mevo lectin towards glycans with terminal alphaMan(1,2)alphaMan structures, and its ability to compromise the internalization of M. tuberculosis in vitro, underscore the potential utility of Mevo lectin as a research tool to study host-pathogen interactions. Mevo lectin specificity towards high-mannose structures with terminal alphaMan(1,2)alphaMan residues and its implication to inhibition of the entry of Mycobacterium tuberculosis into macrophages.,Sivaji N, Harish N, Singh S, Singh A, Vijayan M, Surolia A Glycobiology. 2021 Apr 1. pii: 6207891. doi: 10.1093/glycob/cwab022. PMID:33822039 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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