Interferons are cytokines that play a complex role in the resistance of mammalian hosts to pathogens. IFNγ (interferon-γ) is secreted by activated T-cells and natural killer cells. IFNγ is involved in a wide range of physiological processes, including antiviral activity, immune response, cell proliferation and apoptosis, as well as the stimulation and repression of a variety of genes. IFNγ activity is modulated by the binding of its C-terminal domain to HS (heparan sulphate), a glycosaminoglycan found in the extracellular matrix and at the cell surface. In the present study, we analysed the interaction of isolated heparin-derived oligosaccharides with the C-terminal peptide of IFNγ by NMR, in aqueous solution. We observed marked changes in the chemical shifts of both peptide and oligosaccharide compared with the free state. Our results provide evidence of a binding through electrostatic interactions between the charged side chains of the protein and the sulphate groups of heparin that does not induce specific conformation of the C-terminal part of IFNγ. Our data also indicate that an oligosaccharide size of at least eight residues displays the most efficient binding.
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Research Article|
November 09 2004
NMR characterization of the interaction between the C-terminal domain of interferon-γ and heparin-derived oligosaccharides
Cécile VANHAVERBEKE;
Cécile VANHAVERBEKE
1
*Laboratoire de Résonance Magnétique Nucléaire, Institut de Biologie Structurale CEA-CNRS-UJF ‘J.-P. Ebel’ (UMR CNRS 5075), 41 rue Jules Horowitz, 38027 Grenoble Cedex 1, France
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Jean-Pierre SIMORRE;
Jean-Pierre SIMORRE
*Laboratoire de Résonance Magnétique Nucléaire, Institut de Biologie Structurale CEA-CNRS-UJF ‘J.-P. Ebel’ (UMR CNRS 5075), 41 rue Jules Horowitz, 38027 Grenoble Cedex 1, France
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Rabia SADIR;
Rabia SADIR
†Laboratoire d'Enzymologie Moléculaire, Institut de Biologie Structurale CEA-CNRS-UJF ‘J.-P. Ebel’ (UMR CNRS 5075), 41 rue Jules Horowitz, 38027 Grenoble Cedex 1, France
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Pierre GANS;
Pierre GANS
2
*Laboratoire de Résonance Magnétique Nucléaire, Institut de Biologie Structurale CEA-CNRS-UJF ‘J.-P. Ebel’ (UMR CNRS 5075), 41 rue Jules Horowitz, 38027 Grenoble Cedex 1, France
2To whom correspondence should be addressed (email Pierre.Gans@ibs.fr).
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Hugues LORTAT-JACOB
Hugues LORTAT-JACOB
†Laboratoire d'Enzymologie Moléculaire, Institut de Biologie Structurale CEA-CNRS-UJF ‘J.-P. Ebel’ (UMR CNRS 5075), 41 rue Jules Horowitz, 38027 Grenoble Cedex 1, France
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Publisher: Portland Press Ltd
Received:
May 07 2004
Revision Received:
July 08 2004
Accepted:
July 22 2004
Accepted Manuscript online:
July 22 2004
Online ISSN: 1470-8728
Print ISSN: 0264-6021
The Biochemical Society, London
2004
Biochem J (2004) 384 (1): 93–99.
Article history
Received:
May 07 2004
Revision Received:
July 08 2004
Accepted:
July 22 2004
Accepted Manuscript online:
July 22 2004
Citation
Cécile VANHAVERBEKE, Jean-Pierre SIMORRE, Rabia SADIR, Pierre GANS, Hugues LORTAT-JACOB; NMR characterization of the interaction between the C-terminal domain of interferon-γ and heparin-derived oligosaccharides. Biochem J 15 November 2004; 384 (1): 93–99. doi: https://doi.org/10.1042/BJ20040757
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