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Proteins that bind high-mannose sugars of the HIV envelope

  1. Author:
    Botos, I.
    Wlodawer, A.

  2. Author Address

    NCI, Macromol Crystallog Lab, Frederick, MD 21702 USA Wlodawer, A, NCI, Macromol Crystallog Lab, Bldg 536,Room 5, Frederick, MD 21702 USA
    1. Year: 2005
    2. Date: JUN
  2. Journal: Progress in Biophysics and Molecular Biology
    1. 88
    2. 2
    3. Pages: 233-282
  4. Type of Article: Review
  1. Abstract:

    A broad range of proteins bind high-mannose carbohydrates found on the surface of the envelope protein gp120 of the human immunodeficiency virus and thus interfere with the viral life cycle, providing a potential new way of controlling HIV infection. These proteins interact with the carbohydrate moieties in different ways. A group of them interacts as typical C-type lectins via a Ca2+ ion. Another group interacts with specific single, terminal sugars, without the help of a metal cation. A third group is involved in more intimate interactions, with multiple carbohydrate rings and no metal ion. Finally, there is a group of lectins for which the interaction mode has not yet been elucidated. This review summarizes, principally from a structural point of view, the current state of knowledge about these high-mannose binding proteins and their mode of sugar binding. Published by Elsevier Ltd

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  2. DOI: 10.1016/j.pbiomolbio.2004.05.001
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