Summary: Culture supernates containing pertussis toxin (PT) from four strains of Bordetella pertussis were examined for both immunological reactivity and biological activity. PT from all four strains sensitized mice to histamine and toxin was detectable in supernates of all strains when examined by Western blotting with polyclonal antiserum to PT. In supernates of three of the four strains, PT was detectable by an enzyme-linked immunosorbent assay (ELISA) using mouse monoclonal antibody to subunit S1 of PT as the third antibody layer. However, supernates from one strain, 18323, failed to react in ELISA. Electroblots probed with the monoclonal antibody labelled subunit S1 of PT from all strains except that of strain 18323. PT of strain 18323, whilst retaining histamine-sensitizing activity, differed antigenically from that of other strains.
Summary: A comparative study was made of the virulence and immunogenicity in mice or guinea pigs of Bacillus anthracis strains harbouring 110 MDa and/or 60 MDa plasmids. Strains cured of the 110 MDa or the 60 MDa plasmid were more than 100-fold less virulent to mice than were the parental strains harbouring these plasmids. Guinea-pigs immunized with plasmid-free derivatives of the non-encapsulated vaccine strain 34F2 showed no resistance to challenge with strain 17JB, which harbours both 110 MDa and 60 MDa plasmids, suggesting that the derivative strains had lost their immunizing ability against anthrax.
Summary: Adenylate kinase (ATP:AMP phosphotransferase, EC 188.8.131.52) was detected in partially purified preparations of cell-free extracts of Mycobacterium leprae. The apparent K m values of M. leprae adenylate kinase for ADP and Mg2+ were 1 x 10−4 m and 4 x 10−4 m, respectively. The enzyme was heat-labile: loss of activity by 80% at 45°C and over 90% at 60°C occurred within 5 min. M. leprae adenylate kinase was distinct from armadillo adenylate kinase in respect of affinity for substrate and heat-sensitivity.
Summary: Two DNA fragments, one encoding the Escherichia coli trc promoter and the other encoding a sequence from the early region of Bacillus subtilis phage SPO1, were cloned into the B. subtilis promoter-probe vector pPL603. Both fragments effected strong in vivo promoter activity in vegetative B. subtilis cells.