Epitope mapping of a monoclonal antibody which binds HIV‐1 Gag and not the Gag‐derived proteins

FEBS Letters

Sarubbi, Edoardo¹  Denaro, Maurizio¹ 

[1] Lepetit Research Center, Marion Merrell Dow Research Institute, 21040 Gerenzano, VA, Italy

关键词: Human immunodeficiency virus;    Aspartic protease;    Gag polyprotein;    Monoclonal antibody;    Epitope mapping;    HIV-1;    human immunodeficiency virus type 1;    AIDS;    acquired immunodeficiency syndrome;    ELISA;    enzyme-linked immunosorbent assay;    BSA;    bovine serum albumin;    PBS;    phosphatebuffered saline;    SDS-PAGE;    sodium dodecyl sulphate-polyacrylamide gel electrophoresis;   

DOI  :  10.1016/0014-5793(93)80413-O

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown