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Probing the structure of HIV‐1 Rev by protein footprinting of multiple monoclonal antibody‐binding sites
Author(s) -
Jensen Torben Heick,
Jensen Allan,
Szilvay Anne Marie,
Kjems Jørgen
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00988-5
Subject(s) - footprinting , monoclonal antibody , epitope , binding site , human immunodeficiency virus (hiv) , chemistry , microbiology and biotechnology , computational biology , biology , antibody , virology , biochemistry , genetics , transcription factor , gene
Human immunodeficiency virus type 1 (HIV‐1) Rev is a small RNA‐binding protein which is essential for viral replication. To investigate the structure of Rev we have mapped the binding sites of a panel of monoclonal antibodies (mAb) by protein footprinting and identified a mAb protecting amino acids within both the N‐ and C‐terminal parts of Rev. Our mapping results support a previously proposed structure (Auer et al., Biochemistry , 33 (1994) 2988–2996) predicting that a helix–loop–helix motif in Rev brings the termini of the protein into proximity. Furthermore, we demonstrate that the binding sites mapped by protein footprinting are in agreement with conventional epitope mapping results and that this technique provides an advantageous strategy for mapping discontinuous sites.