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Structure type: fragment of a bigger structure
Trivial name: linear B, α-Gal epitope
Contained glycoepitopes: IEDB_115013,IEDB_130645,IEDB_136044,IEDB_136906,IEDB_137472,IEDB_141794,IEDB_149558,IEDB_151528,IEDB_190606,IEDB_918314,SB_165,SB_166,SB_187,SB_195,SB_7,SB_87,SB_88

• Article ID: 4666
  Brockhausen I "Crossroads between Bacterial and Mammalian Glycosyltransferases" - Frontiers in Immunology 5 (2014) 492
  

  Bacterial glycosyltransferases (GT) often synthesize the same glycan linkages as mammalian GT; yet, they usually have very little sequence identity. Nevertheless, enzymatic properties, folding, substrate specificities, and catalytic mechanisms of these enzyme proteins may have significant similarity. Thus, bacterial GT can be utilized for the enzymatic synthesis of both bacterial and mammalian types of complex glycan structures. A comparison is made here between mammalian and bacterial enzymes that synthesize epitopes found in mammalian glycoproteins, and those found in the O antigens of Gram-negative bacteria. These epitopes include Thomsen-Friedenreich (TF or T) antigen, blood group O, A, and B, type 1 and 2 chains, Lewis antigens, sialylated and fucosylated structures, and polysialic acids. Many different approaches can be taken to investigate the substrate binding and catalytic mechanisms of GT, including crystal structure analyses, mutations, comparison of amino acid sequences, NMR, and mass spectrometry. Knowledge of the protein structures and functions helps to design GT for specific glycan synthesis and to develop inhibitors. The goals are to develop new strategies to reduce bacterial virulence and to synthesize vaccines and other biologically active glycan structures.

  glycosyltransferases, protein structure, specificities, glycoprotein epitopes, glycan mimics

  Publication DOI: 10.3389/fimmu.2014.00492
  Journal NLM ID: 101560960
  Publisher: Lausanne: Frontiers Research Foundation
  Correspondence: brockhau@queensu.ca
  Institutions: Department of Biomedical and Molecular Sciences, Queen's University, Kingston, ON, Canada, Department of Biomedical and Molecular Sciences, Queen's University, 18 Stuart Street, Kingston, ON K7L3N6
  
   
  
  Neisseria meningitidis
  CSDB ID 30219 (all data & tools)
• Article ID: 5915
  de Souza LMB, Soccol VT, Petterle RR, Bates MD, Bates PA "Analysis of Leishmania mimetic neoglycoproteins for the cutaneous leishmaniasis diagnosis" - Parasitology 145(14) (2018) 1938-1948
  

  Oligosaccharides are broadly present on Leishmania cell surfaces. They can be useful for the leishmaniases diagnosis and also helpful in identifying new cell markers for the disease. The disaccharide Galα1-3Galβ is the immunodominant saccharide in Leishmania cell surface and is the unique non-reducing terminal glycosphingolipids structure recognized by anti-α-Gal. This study describes an enzyme-linked immunosorbent assay (ELISA) used to measure serum levels of anti-α-galactosyl (α-Gal) antibodies in patients with cutaneous leishmaniasis (CL). Optimal ELISA conditions were established and two neoglycoproteins (NGP) containing the Galα1-3Gal terminal fraction (Galα1-3Galβ1-4GlcNAc-HAS and Galα1-3Gal-HAS) and one Galα1-3Gal NGP analogue (Galα1-3Galβ1-3GlcNAc-HAS) were used as antigens. Means of anti-α-Gal antibody titres of CL patients were significantly higher (P < 0.05) than the healthy individuals for all NGPs tested. Sensitivity and specificity of all NGPs ranged from 62.2 to 78.4% and 58.3 to 96.7%, respectively. In conclusion, the NGPs can be used for CL diagnosis.

  antigen, ELISA, saccharide, α-galactosyl, L.braziliensis

  NCBI PubMed ID: 29806570
  Publication DOI: 10.1017/S0031182018000720
  Journal NLM ID: 0401121
  Publisher: London, New York, Cambridge University Press
  Correspondence: p.bates@lancaster.ac.u
  Institutions: Laboratory of Molecular Biology, Department of Bioprocess Engineering and Biotechnology, Universidade Federal do Paraná, Avenida Coronel Francisco Heráclito dos Santos, 210 - Usina Piloto B, Curitiba, Paraná 81531-970, Brazil, Nucleus of Medical Education, Department of Community Health, Universidade Federal do Paraná, Rua Padre Camargo, 280 - 7th floor, Curitiba, Paraná 80060-240, Brazil, Division of Biomedical and Life Sciences, Faculty of Health and Medicine,Lancaster University, Lancaster, Lancashire, LA1 4YQ,UK
  Methods: ELISA, antibody binding, statistical analysis
  
   
  
  Leishmania
  CSDB ID 7285 (all data & tools)