Proteins that bind high-mannose sugars of the HIV envelope.
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.
Botos
Istvan
I
Macromolecular Crystallography Laboratory, National Cancer Institute, NCI-Frederick, Building 536, Room 5, Frederick, MD 21702-1201, USA.
Wlodawer
Alexander
A
D000818:Animals; D001665:Binding Sites; D002352:Carrier Proteins / Q000737:chemistry / Q000378:metabolism; D006678:HIV / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D037601:Mannose-Binding Lectin / Q000737:chemistry* / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D014759:Viral Envelope Proteins / Q000737:chemistry / Q000378:metabolism; D014760:Viral Fusion Proteins / Q000737:chemistry* / Q000378:metabolism*
D002352:Carrier Proteins; D037601:Mannose-Binding Lectin; D014759:Viral Envelope Proteins; D014760:Viral Fusion Proteins