SUMMARYHindlII fragments D to P of DNA from a Chinese vaccine strain (Tian Tan) of vaccinia virus have been molecularly cloned into the plasmid pAT153 at the unique HindlII site. The Chinese strain DNA differs from a non-vaccine American strain (WR) in having an additional HindlII fragment (P). Twelve HindlII D clones and 12 HindlII F clones of the Chinese strain were analysed by digestion by EcoRI, BamHI, PstI and XhoI. Two forms of D (designated a and b) and of F (a and b) were demonstrated. In each the differences were detected as the presence of an additional EcoRI site, in Da and Fa. The HindlII Fa and Fb fragments of the Chinese strain were shown to differ significantly from the WR strain in their restriction site maps.In recent years, interest has arisen in the use of the vaccinia virus genome as a eukaryotic expression vector for the construction of live recombinant vaccines directed against both human and veterinary infectious diseases or for the synthesis of biological products. Panicali & Paoletti (1982), Panicali et al. (1983) and Mackett et al. (1982) successfully adapted site-specific recombination between the HindlII F or J fragments of vaccinia virus DNA flanking the foreign DNA and homologous sequences in replicating viral DNA to allow insertion of the foreign DNA into infectious progeny. Biological activity of recombinant vaccinia virus expressing hepatitis B virus surface antigen (Smith et al., 1983), influenza virus haemagglutinin (Panicali et al., 1983) and herpes simplex virus thymidine kinase (Panicali & Paoletti, 1982) have been demonstrated. These authors, however, used the Western Reserve (WR) strain of vaccinia virus, which has not been used for human vaccination. The safety of the recombinant vaccinia viruses as human live vaccines awaits further investigation. In this paper we describe the cloning of the HindlII fragments D to P of the Chinese Tian Tan strain of vaccinia virus, the variation in the HindlII D and F fragments, and the distinct restriction map of the HindlII F fragment of the Tian Tan strain, as compared with that of the WR strain.
Two protease inhibitors (Inh2 and Inh3) from bovine plasma have been isolated and characterized. The apparent molecular weights of the two proteins are 56 and 58 kDa, respectively. Although Inh2 and Inh3 both inhibit trypsin and human neutrophil elastase, only Inh3 is a good inhibitor of chymotrypsin and cathepsin G. Inh3 is much more sensitive to oxidation than Inh2. One murine monoclonal antibody recognizes Inh3 but not Inh2. Inh3 resembles human alpha 1-antitrypsin both structurally and functionally. Inh2, on the other hand, has some structural homology to human alpha 1-antichymotrypsin, but its specificity does not correspond to that of either human alpha 1-antitrypsin or human alpha 1-antichymotrypsin.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
hi@scite.ai
10624 S. Eastern Ave., Ste. A-614
Henderson, NV 89052, USA
Copyright © 2024 scite LLC. All rights reserved.
Made with 💙 for researchers
Part of the Research Solutions Family.