Chemical terror is one of the main forms of terrorism. The proliferation of chemical weapon and abuse of chemical poisons make chemical terrorism flourish and diversified in occurrence. The features of chemical terrorism are unexpectedness, surreptitiousness, diversity in their vehicles and media, and it could be widespread to involve a broad area to create a serious tumult. Medical protection is the pivotal step to control the influence of chemical terror. Anti-chemical terror medicine will provide new important subjects for researches in chemical-defense medicine, and studies in chemical-defense medicine will lay the foundation of anti-chemical-terror medicine. In conclusion, it is imperative that the principles, main subjects, and strategies of research on anti-chemical-terror medicine should be established as early as possible.

Objective:To express Gag gp120 fusion protein in the recombinant fowlpox virus.Methods:The Gag gp120 gene of HIV 1 was inserted downstream of the combined promoter in pUTAL,an expressing plasmid was constructed.By transfecting the plasmid into CEF cells pre infected with FPV 282E 4 strain,a recombinant fowlpox virus vUTALG was obtained by selecting in the presence of BUdR and subsequent blue plaque screening.Results:Western blot showed that the recombinant virus expressed the Gag gp120 fusion protein in the infected CEF cells.The virus like particles formed by Gag protein were observed under electron microscope.Mice were immunized with the recombinant virus.The results showed the recombinant virus could induce HIV 1 specific antibody response.Conclusion:The recombinant fowlpox virus could express the Gag gp120 fusion protein.

A fragment of chalcone synthase gene (SmCHS) was cloned from the cDNA library constructed in Saussurea medusa. The full-length cDNA sequence of SmCHS was obtained by RT-PCR. Sequence analysis showed that the full length of SmCHS was 1313 bp, containing an open reading frame (1170 bp) encoding 389 amino acids. The molecular weight of the protein was estimated to be 43 kDa. The prokaryotic expression plasmids pET28a(+)-SmCHS was constructed and transformed into Escherichia coli BL21(DE3) for expression. SDS-PAGE indicated that the fusion protein was expressed partially in soluble form after induction by IPTG. The recombinant protein was collected and purified by Ni-NTA affinity column. The enzymatic activity assay of the purified recombinant protein showed that the fusion protein had chalcone synthase activity. It could catalyze the condensation of a 4-coumaroyl-CoA with three malonyl-CoAs to produce naringenin chalcone.
Acyltransferases ; genetics ; metabolism ; Amino Acid Sequence ; Catalysis ; Chalcones ; biosynthesis ; Cloning, Molecular ; DNA, Complementary ; genetics ; Escherichia coli ; genetics ; metabolism ; Genetic Vectors ; genetics ; Molecular Sequence Data ; Plant Proteins ; genetics ; metabolism ; Recombinant Proteins ; genetics ; metabolism ; Saussurea ; enzymology ; genetics