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The plant ribosome inactivating proteins luffin and saporin are potent inhibitors of HIV‐1 integrase
Author(s) -
Au T.K,
Collins R.A,
Lam T.L,
Ng T.B,
Fong W.P,
Wan D.C.C
Publication year - 2000
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(00)01389-2
Subject(s) - ribosome inactivating protein , integrase , saporin , protease , ribosome , biology , reverse transcriptase , in vitro , virology , microbiology and biotechnology , chemistry , biochemistry , enzyme , rna , human immunodeficiency virus (hiv) , immunotoxin , cytotoxicity , gene
The ribosome inactivating proteins (RIPs) are a group of proteins that are able to inactivate eukaryotic protein synthesis by attacking the 28S ribosomal RNA. Recent studies have shown that some RIPs possess strong anti‐human immunodeficiency virus (HIV) activity. In this study, several common plant RIPs including agrostin, gelonin, luffin, α‐momorcharin, β‐momorcharin, saporin and trichosanthin were examined for the ability to interfere with HIV‐1 replication in a variety of mechanistic assays in vitro. These assays included the CD4/gp120 interaction assay, HIV‐1 reverse transcriptase (RT) assay, HIV‐1 protease assay and HIV‐1 integrase assay. At the concentration of 100 nM, all RIPs appeared to enhance the CD4/gp120 interaction by about 50%. These RIPs exhibited a very weak suppressive effect on HIV‐1 RT and on HIV‐1 protease. In contrast, with the exception of agrostin, all the RIPs tested could strongly inhibit HIV‐1 integrase, the extent of inhibition ranging from 26.1 to 96.3% in an ELISA‐based assay. Two RIPs, saporin and luffin, which licited over 90% inhibition in the ELISA‐based assay, were further characterized in a radiometric assay. Both of these two RIPs evoked a strong dose‐dependent inhibition in the 3′‐end processing and strand‐transfer activities of integrase. The results from this study suggest that the anti‐HIV property of RIPs may be due to inhibition of HIV‐1 integrase.