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A structural motif in the variant surface glycoproteins of Trypanosoma brucei

Nature volume 362, pages 603609 (15 April 1993) | Download Citation

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Abstract

The variable domain of the trypanosome variant surface glycoprotein (VSG) ILTat 1.24 has been shown by X-ray crystallography to resemble closely the structures of VSG MITat 1.2, despite their low sequence similarity. Specific structural features of these VSGs, including substitution of carbohydrate for an α-helix, can be found in other VSG sequences. Thus antigenic variation in trypanosomes is accomplished by sequence variation, not gross structural alteration; the extensive sequence differences among VSGs may be required for another reason, such as the avoidance of recognition by helper T cells. Additionally, VSG sequences are found to define families, within a VSG superfamily, which have evolved in the trypanosome genome.

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Author information

Affiliations

  1. Howard Hughes Medical Institute, Harvard University, 7 Divinity Avenue, Cambridge, Massachusetts 02138, USA

    • Don C. Wiley
  2. Department of Biochemistry and Molecular Biology, Harvard University, 7 Divinity Avenue, Cambridge, Massachusetts 02138, USA

    • Michael L. Blum
    • , James A. Down
    •  & Don C. Wiley
  3. Merck Sharpe & Dohme, Research Laboratories, Box 2000, Rahway, New Jersey 07065, USA

    • Anne M. Gurnett
    •  & Mervyn J. Turner
  4. Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB21QW, UK

    • Mark Carrington
  5. Present addresses: Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA (M.L.B.); Beckton Dickinson and Company, Research Center, Box 12016, Research Triangle Park, North Carolina 27709, USA (J.A.D.).

    • Michael L. Blum
    •  & James A. Down

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https://doi.org/10.1038/362603a0

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