Solution structure of two xeno-antigens: aGal-LacNAc and aGal-Lewis X

  1. Corzana, F. 12
  2. Bettler, E. 1
  3. Du Penhoat, C.H. 1
  4. Tyrtysh, T.V. 3
  5. Bovin, N.V. 3
  6. Imberty, A. 1
  1. 1 Joseph Fourier University
    info

    Joseph Fourier University

    Grenoble, Francia

    ROR https://ror.org/02aj0kh94

  2. 2 Universidad de La Rioja
    info

    Universidad de La Rioja

    Logroño, España

    ROR https://ror.org/0553yr311

  3. 3 Russian Academy of Sciences
    info

    Russian Academy of Sciences

    Moscú, Rusia

    ROR https://ror.org/05qrfxd25

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Revista:
Glycobiology

ISSN: 0959-6658

Año de publicación: 2002

Volumen: 12

Número: 4

Páginas: 241-250

Tipo: Artículo

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PMID: 12042247 SCOPUS: 2-s2.0-0036019909 WoS: WOS:000176362200005 GOOGLE SCHOLAR

Otras publicaciones en: Glycobiology

Repositorio institucional: lock_openAcceso abierto Editor

Resumen

Organ hyperacute rejection, a phenomenon occurring during discordant xenotransplantation, is due to the recognition of an oligosaccharide epitope by human xenoreactive natural antibodies. In addition to the αGal(1-3)βGal(1-4)GlcNAc trisaccharide, a fucosylated structure, αGal-Lewis X, has been shown to be recognized by the antibodies. Both the trisaccharide and the tetrasaccharide have been synthesized by chemical methods. A complete nuclear magnetic resonance characterization of the two compounds has been performed, including the measurements of two-dimensional nuclear Overhauser effect spectroscopy data. Molecular dynamics simulations were run for several ns in the presence of explicit water molecules. The combination of experimental and theoretical approaches revealed the effect of an additional fucose residue on the conformational behavior of the xenoantigen. This branched fucose strongly rigidifies the N-acetyllactosamine. The effect on the αGal(1-3)Gal fragment is less marked. In the presence of fucose, the terminal αGal residue can still adopt two different conformations, but the equilibrium populations are modified.