Caseous lymphadenitis vaccine development: site-specific inactivation of the Corynebacterium pseudotuberculosis phospholipase D gene.

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
• Journal: Vaccine (Vaccine) Vol. 13 Issue 18 Pg. 1785-92 (Dec 1995) ISSN: 0264-410X [Print] Netherlands
• 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