Why human anti-Galα1–4Galβ1–4Glc natural antibodies do not recognize the trisaccharide on erythrocyte membrane? Molecular dynamics and immunochemical investigation

Molecular Immunology

Volumn 90, Issue , 2017, Pages 87-97

  Volynsky, Pavel ^a   Efremov, Roman ^a,b   Mikhalev, Ilya ^a   Dobrochaeva, Kira ^a   Tuzikov, Alexander ^a   Korchagina, Elena ^a   Obukhova, Polina ^a   Rapoport, Evgenia ^a   Bovin, Nicolai ^a  

^a SHEMYAKIN OVCHINNIKOV INSTITUTE OF BIOORGANIC CHEMISTRY   (Russian Federation)

^b NATIONAL RESEARCH UNIVERSITY HIGHER SCHOOL OF ECONOMICS   (Russian Federation)

Author keywords

Epitope; Gb3Cer; Glycan; Glycolipid; Molecular dynamics simulation; Natural antibodies

Indexed keywords

2 OLEOYL 1 PALMITOYLPHOSPHATIDYLCHOLINE; ANTIBODY; GLOBOTRIAOSYLCERAMIDE; GLYCAN; GLYCOLIPID; IMMUNOGLOBULIN A ANTIBODY; IMMUNOGLOBULIN G ANTIBODY; IMMUNOGLOBULIN M ANTIBODY; SOLVENT; TRISACCHARIDE; ARTIFICIAL MEMBRANE; CERAMIDE TRIHEXOSIDE; EPITOPE; GLOBOTRIOSE;

ADULT; ANIMAL CELL; ARTICLE; CONFORMATION; ENZYME LINKED IMMUNOSORBENT ASSAY; ERYTHROCYTE; ERYTHROCYTE MEMBRANE; FLOW CYTOMETRY; FLUORESCENCE ACTIVATED CELL SORTING; HUMAN; IMMUNOCHEMISTRY; LIPID BILAYER; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; VERO CELL LINE; ANIMAL; ARTIFICIAL MEMBRANE; CELL LINE; CHLOROCEBUS AETHIOPS; IMMUNOLOGY;

ANIMALS; ANTIBODIES; CELL LINE; CERCOPITHECUS AETHIOPS; EPITOPES; ERYTHROCYTE MEMBRANE; GLYCOLIPIDS; HUMANS; MEMBRANES, ARTIFICIAL; MOLECULAR DYNAMICS SIMULATION; TRIHEXOSYLCERAMIDES; TRISACCHARIDES; VERO CELLS;

EID: 85021889822     PISSN: 01615890     EISSN: 18729142     Source Type: Journal    
DOI: 10.1016/j.molimm.2017.06.247     Document Type: Article

References (27)

1. Abraham, M.J., Murtola, T., Schulz, R., Páll, S., Smith, J.C., Hess, B., Lindahl, E., GROMACS: High performance molecular simulations through multi-level parallelism from laptops to supercomputers. SoftwareX 1:-2 (2015), 19–25.
2. Berendsen, H.J.C., Postma, J.P.M., van Gunsteren, W.F., DiNola, A., Haak, J.R., Molecular dynamics with coupling to an external bath. J. Chem. Phys. 81 (1984), 3684–3690.
3. Bovin, N., Obukhova, P., Shilova, N., Rapoport, E., Popova, I., Navakouski, M., Unverzagt, C., Vuskovic, M., Huflejt, M., Repertoire of human natural anti-glycan immunoglobulins. Do we have auto-antibodies?. Biochim. Biophys. Acta 1820 (2012), 1373–1382.
4. Bovin, N.V., Natural antibodies to glycans. Biochemistry (Moscow) 78 (2013), 786–797.
5. Cheng, A.L., Merz, K.M., Application of the Nosé-Hoover chain algorithm to the study of protein dynamics. J. Phys. Chem. 100 (1996), 1927–1937.
6. Darden, T., York, D., Pedersen, L., Particle mesh Ewald: an N-log(N) method for Ewald sums in large systems. J. Chem. Phys. 98 (1993), 10089–10092.
7. Galili, U., Rachmilewitz, E.A., Peleg, A., Flechner, I., A unique natural human IgG antibody with anti-alpha-galactosyl specificity. J. Exp. Med. 160 (1984), 1519–1531.
8. Giger, U., Sticher, B., Naef, R., Burger, R., Lutz, H.U., Naturally occurring human anti-band 3 autoantibodies accelerate clearance of erythrocytes in guinea pigs. Blood 85:7 (1995), 1920–1928.
9. Hancock, J.F., Lipid rafts: contentious only from simplistic standpoints. Nat. Rev. Mol. Cell Biol. 7 (2006), 456–462.
10. Harrison, A.L., Olsson, M.L., Jones, R.B., Ramkumar, S., Sakac, D., Binnington, B., Henry, S., Lingwood, C.A., Branch, D.R., A synthetic globotriaosylceramide analogue inhibits HIV-1 infection in vitro by two mechanisms. Glycoconj. J. 27 (2010), 515–524.
11. k) locus do not correlate with the presence of the P1 blood group antigen. BMC Genet., 6, 2005, 49.
12. Huflejt, M.E., Vuskovic, M., Vasiliu, D., Xu, H., Obukhova, P., Shilova, N., Tuzikov, A., Galanina, O., Arun, B., Lu, K., Bovin, N., Anti-carbohydrate antibodies of normal sera: findings, surprises and challenges. Mol. Immunol. 46 (2009), 3037–3049.
13. Jämbeck, J.P., Lyubartsev, A.P., Another piece of the membrane puzzle: extending slipids further. J. Chem. Theory Comput. 9 (2013), 774–784.
14. Jorgensen, W.L., Chandrasekhar, J., Madura, J.D., Impey, R.W., Klein, M.L., Comparison of simple potential functions for simulating liquid water. J. Chem. Phys. 79 (1983), 926–935.
15. Khasbiullina, N.R., Bovin, N.V., Hypotheses of the origin of natural antibodies: a glycobiologist's opinion. Biochemistry (Moscow) 80 (2015), 820–835.
16. Korchagina, E.Y., Henry, S.M., Synthetic glycolipidlike constructs as tools for glycobiology research, diagnostics, and as potential therapeutics. Biochemistry (Moscow) 80 (2015), 857–871.
17. Korchagina, E., Tuzikov, A., Formanovsky, A., Popova, I., Henry, S., Bovin, N., Towards creating cell membrane glyco-landscapes with glycan lipid constructs. Carbohydr. Res. 356 (2012), 238–246.
18. Lacroix Desmazes, S., Kaveri, S.V., Mouthon, L., Ayouba, A., Malanchere, E., Coutinho, A., Kazatchkine, M.D., Self-reactive antibodies (natural autoantibodies) in healthy individuals. J. Immunol. Methods 216 (1998), 117–137.
19. Lund, N., Olsson, M.L., Ramkumar, S., Sakac, D., Yahalom, V., Levene, C., Hellberg, A., Ma, X.Z., Binnington, B., Jung, D., Lingwood, C.A., Branch, D.R., The human P(k) histo-blood group antigen provides protection against HIV-1 infection. Blood 113 (2009), 4980–4991.
20. Mikhalev, I.I., Molotkovskiĭ, Iu.G., Synthesis and characteristics of fluorescent BODIPY-labeled gangliosides. Bioorg. Khim. 29 (2003), 190–197.
21. Nasir, W., Frank, M., Kunze, A., Bally, M., Parra, F., Nyholm, P.G., Höök, F., Larson, G., Histo-blood group antigen presentation is critical for binding of Norovirus VLP to glycosphingolipids in model membranes. ACS Chem. Biol. 19 (2017), 1288–1296.
22. Novak, A., Binnington, B., Ngan, B., Chadwick, K., Fleshner, N., Lingwood, C.A., Cholesterol masks membrane glycosphingolipid tumor-associated antigens to reduce their immunodetection in human cancer biopsies. Glycobiology 23 (2013), 1230–1239.
23. Obukhova, P., Rieben, R., Bovin, N., Normal human serum contains high levels of anti-Galalpha1-4GlcNAc antibodies. Xenotransplantation 14 (2007), 627–635.
24. Parrinello, M., Rahman, A., Polymorphic transitions in single crystals: a new molecular dynamics method. J. Appl. Phys. 52 (1981), 7182–7190.
25. Spitalnik, P.F., Spitalnik, S.L., The P blood group system: biochemical, serological, and clinical aspects. Transfus. Med. Rev. 9 (1995), 110–122.
26. Taguchi, H., Planque, S., Nishiyama, Y., Symersky, J., Boivin, S., Szabo, P., Friedland, R.P., Ramsland, P.A., Edmundson, A.B., Weksler, M.E., Paul, S., Autoantibody-catalyzed hydrolysis of amyloid beta peptide. J. Biol. Chem. 283:8 (2008), 4714–4722.
27. Watkins, E.B., Gao, H., Dennison, A.J., Chopin, N., Struth, B., Arnold, T., Florent, J.C., Johannes, L., Carbohydrate conformation and lipid condensation in monolayers containing glycosphingolipid Gb3: influence of acyl chain structure. Biophys. J. 107 (2014), 1146–1155.