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Isolation and characterization of anti‐HIV peptides from Dorstenia contrajerva and Treculia obovoidea
Author(s) -
Bokesch Heidi R.,
Charan Romila D.,
Meragelman Karina M.,
Beutler John A.,
Gardella Roberta,
O'Keefe Barry R.,
McKee Tawnya C.,
McMahon James B.
Publication year - 2004
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/j.febslet.2004.04.085
Subject(s) - chemistry , human immunodeficiency virus (hiv) , isolation (microbiology) , biochemistry , biology , virology , microbiology and biotechnology
Using a high throughput screen based on the interaction of the HIV‐1 gp41 ectodomain with the virucidal protein cyanovirin‐N (CV‐N), we isolated two new peptides which inhibited the binding of CV‐N to gp41 and which subsequently showed anti‐HIV activity in a whole cell assay. A 5‐kDa (contrajervin) and 10 kDa (treculavirin) peptide were isolated from Dorstenia contrajerva and Treculia obovoidea , respectively. Treculavirin was composed of two subunits, each containing 50 amino acid residues, which are covalently linked by at least one disulfide bond between the subunits. Both peptides were shown to bind to gp41 and gp120 and to inhibit the cytopathic effects of HIV‐1 RF infection in a human T‐lymphoblastoid cell line (CEM‐SS).