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Epitope mapping of a monoclonal antibody which binds HIV‐1 Gag and not the Gag‐derived proteins
Author(s) -
Sarubbi Edoardo,
Denaro Maurizio
Publication year - 1993
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 - 10.1016/0014-5793(93)80413-o
Subject(s) - epitope , monoclonal antibody , cleavage (geology) , protease , proteolysis , microbiology and biotechnology , chemistry , binding site , epitope mapping , antibody , group specific antigen , virology , biology , biochemistry , human immunodeficiency virus (hiv) , enzyme , genetics , paleontology , fracture (geology)
Monoclonal antibody (MAb) 1G12 binds the uncleaved HIV‐1 Gag polypeptide (p55), but fails to recognize the final products of the proteolytic processing [Sarubbi, E. et al. (1991) FEBS Lett. 279, 265‐269]. In this report we show that binding of MAb 1G12 to a 110‐residue Gag fragment containing the p17–p24 cleavage site prevents proteolysis of this site by the HIV‐1 protease. Competition studies with synthetic peptides have been performed to map the binding site of MAb 1G12 on Gag. The antibody recognizes a sequential epitope that spans the HIV‐1 protease cleavage site; determinants located on both p17 and p24 are required for antibody binding. MAb 1G12 is also shown to lack any cross‐reactivity with other HIV‐1 protease cleavage sites.