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A new class of anti‐HIV agents: GAP31, DAPs 30 and 32
Author(s) -
Lee-Huang Sylvia,
Kung Hsiang-fu,
Huang Paul L.,
Huang Philip L.,
Li Bao-Qun,
Huang Peter,
Huang Henry I.,
Chen Hao-Chia
Publication year - 1991
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(91)81122-o
Subject(s) - amino acid , biology , homology (biology) , carnation , human immunodeficiency virus (hiv) , biochemistry , peptide sequence , virology , gene , botany
Three inhibitors of human immunodeficiency virus (HIV) have been isolated and purified to homogeneity from Euphorbiaceae himalaya seeds ( Gelonium multiflorum ) and carnation leaves ( Dianthus caryophytlus ). These proteins. GAP 31 (Gelonium Anti‐HIV Protein 31 kDa) and DAPs 30 and 32 (dianthus anti‐HIV proteins, 30 and 32 kDa), inhibit HIV‐1 infection and replication in a dosc‐dependent manner with little toxicity to target cells. The therapeutic indices of these compounds are in the order 10 4 , suggesting that they may be clinically important agents in the treatment of AIDS. The N‐terminal amino acid sequences of these proteins show little homology to those of previously described anti‐HIV proteins. The structure‐function features of these HIV inhibitors, based on the 40–60 amino acid residues of N‐terminal sequences, are examined.