期刊论文详细信息
FEBS Letters
The plant ribosome inactivating proteins luffin and saporin are potent inhibitors of HIV‐1 integrase
Wan, D.C.C1  Fong, W.P1  Lam, T.L1  Collins, R.A1  Au, T.K1  Ng, T.B1 
[1] Department of Biochemistry, The Chinese University of Hong Kong, Shatin, New Territories, Hong Kong, China
关键词: HIV-1;    Ribosome inactivating protein;    Integrase;    Protease;    Reverse transcriptase;    CD4/gp120;    HIV-1;    human immunodeficiency virus type 1;    BSA;    bovine serum albumin;    PBS;    phosphate-buffered saline;   
DOI  :  10.1016/S0014-5793(00)01389-2
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 摘 要 】

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.

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