| Abstract | Vaccines for ovine caseous lymphadenitis (CLA) are currently formulated using partially purified, formalin inactivated phospholipase D (PLD) derived from Corynebacterium pseudotuberculosis culture supernatants. Chemical treatment has been a common and effective way of inactivating bacterial toxins for use in toxoid vaccines. Genetic inactivation of toxin genes using site-specific mutagenesis has the potential to improve this process by providing a safer and more cost-effective product. In the present study amino acid substitutions at the putative catalytic site and metal binding domain of the PLD protein had a profound affect upon PLD activity and secretion from C. pseudotuberculosis. Two mutated PLD analogues that were secreted to a level of 40% compared to the wild-type and retained minimal activity showed promise for development as recombinant CLA vaccines. Further work will be required to establish their suitability for commercialization. |
| Authors | M Tachedjian, J Krywult, R J Moore, A L Hodgson
(Affiliation: CSIRO Division of Animal Health, Animal Health Research Laboratory, Parkville, Victoria, Australia.)
|
| Journal | Vaccine
(Vaccine)
Vol. 13
Issue 18
Pg. 1785-92
(Dec 1995)
ISSN: 0264-410X ENGLAND |
| PMID | 8701594
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
|
| Chemical References |
- Bacterial Vaccines
- Formaldehyde
- Phospholipase D
|
| Topics |
- Animals
- Bacterial Vaccines
(immunology)
- Base Sequence
- Corynebacterium Infections
(prevention & control, veterinary)
- Corynebacterium pseudotuberculosis
(genetics)
- Formaldehyde
- Lymphadenitis
(immunology, veterinary)
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Phospholipase D
(genetics)
- Sheep
|
