1988
DOI: 10.1016/0378-1119(88)90439-8
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Sequence and analysis of the DNA encoding protective antigen of Bacillus anthracis

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Cited by 159 publications
(103 citation statements)
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“…For construction of anthrax toxin-Hoc fusion recombinants, the T7 expression plasmids, pET-15b (Amp r ) and pET-28b (Kan r ) (EMD Biosciences, Inc) were used as cloning vectors. Plasmids pPA26, pLF7 (LF-E687C) 2 , pEF-K346R and purified phage T4 genomic DNA were used as templates for amplification of the PA gene (pagA) [20], LF gene (lef) [21], EF gene (cya), [22] and Hoc gene respectively. E. coli XL-10 Gold was used for initial transformation and E. coli codon-plus BL21 (DE3) RIL/ RIPL (Stratagene) was used for IPTG-induced over-expression of toxin-Hoc fusion proteins [23].…”
Section: Bacteriophage Bacteria and Plasmidsmentioning
confidence: 99%
“…For construction of anthrax toxin-Hoc fusion recombinants, the T7 expression plasmids, pET-15b (Amp r ) and pET-28b (Kan r ) (EMD Biosciences, Inc) were used as cloning vectors. Plasmids pPA26, pLF7 (LF-E687C) 2 , pEF-K346R and purified phage T4 genomic DNA were used as templates for amplification of the PA gene (pagA) [20], LF gene (lef) [21], EF gene (cya), [22] and Hoc gene respectively. E. coli XL-10 Gold was used for initial transformation and E. coli codon-plus BL21 (DE3) RIL/ RIPL (Stratagene) was used for IPTG-induced over-expression of toxin-Hoc fusion proteins [23].…”
Section: Bacteriophage Bacteria and Plasmidsmentioning
confidence: 99%
“…This could mean that the mechanism by which iota-toxin enters the cell could be different as compared with that of C2 toxin because it has convincingly been demonstrated that either endocytosis or acidification of the environment is essential for intoxication of target cells in the case of C2 toxin of C. botulinum (23,24). On the other hand, it has also been demonstrated that the binding components of C2 toxin, iotatoxin, and the anthrax protective antigen share common structural properties, which suggests a common mode of action (11,22,25,26).…”
mentioning
confidence: 99%
“…In Fig. 2(a), a schematic of fragments of PA83 generated by trypsin and chymotrypsin digestion based on the sequences and mapping studies previously described [16,17] is shown. Intact PA83, trypsin, chymotrypsin or combination of trypsin and chymotrypsin generated PA fragments were probed with human monoclonal antibodies AVP-1C6, AVP-22G12 and AVP-21D9 in a western blot (Fig.…”
Section: Methodsmentioning
confidence: 99%