Your browser version may not work well with NCBI's Web applications. More information here...
1: Biochem Biophys Res Commun. 2003 Sep 26;309(3):598-604.Click here to read Links

Molecular characterization of Trimeresurus stejnegeri venom L-amino acid oxidase with potential anti-HIV activity.

Zhang YJ, Wang JH, Lee WH, Wang Q, Liu H, Zheng YT, Zhang Y.

Department of Animal Toxinology, Kunming Institute of Zoology, The Chinese Academy of Sciences, Kunming, Yunnan 650223, China.

A novel L-amino acid oxidase, named TSV-LAO, has been purified and cloned from the snake Trimeresurus stejnegeri. Fifty percentage cytotoxic concentrations (CC50) of TSV-LAO on C8166 cells were 24 and 390 nM in the absence or presence of catalase (400 nM), respectively. However, at concentrations that showed little effect on cell viability, TSV-LAO displayed dose dependent inhibition on HIV-1 infection and replication. The antiviral selectivity indexes (CC50/EC50) were 16 and 6, respectively, corresponding to the measurements of syncytium formation and HIV-1 p24 antigen expression. Interestingly, the presence of catalase resulted in an increase of its antiviral selectivity to 52 and 38. Under the same conditions, no anti-HIV-1 activity was observed by exogenous addition of H2O2. The complete amino acid sequence of TSV-LAO, as deduced from its cDNA, exhibits a high degree of sequence identity with other snake venom LAOs.

PMID: 12963032 [PubMed - indexed for MEDLINE]