The 20 kDa C-terminally truncated form of pertussis toxin subunit S1 secreted from Bacillus subtilis
- 15 March 1991
- journal article
- Published by Oxford University Press (OUP) in FEMS Microbiology Letters
- Vol. 79 (1) , 115-120
- https://doi.org/10.1016/0378-1097(91)90538-l
Abstract
The subunit S1 of pertussis toxin (PT) was purified as the recombinant product BacS1 from the culture supernatant of a Bacillus subtilis strain containing a secretion vector with a DNA fragment coding for the mature subunit S1 inserted downstream of the signal sequence of the α-amylase gene. The method of purification was successive ion exchange and adsorption chromatography. BacS1 occurred in two forms (28 and 20 kDa) of which the truncated 20-kDa peptide was the main one in the supernatant. The truncated BacS1 was purified and shown to have the same NH2-terminus as the full-size (28 kDa) BacS1. It was also enzymatically active indicating correct conformation. The truncated BacS1 was also shown to elicit neutralizing and protective antibodies when injected into mice or rabbits.Keywords
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