02088naa a2200385 a 450000100080000000500110000800800410001902400390006010000190009924501610011826000090027952009710028865000230125965000260128265000170130865000200132565000230134565000150136865000200138365000100140365000110141365000240142465000110144865000110145965300180147065300250148865300160151365300190152965300200154865300280156870000160159670000170161270000210162977300520165015241172023-08-03       1995    bl uuuu     u00u1 u    #d7 a10.1016/0264-410x(95)00144-p.2DOI1 aTACHEDJIAN, M.  aCaseous lymphadenitis vaccine developmentbsite-specific inactivation of the Corynebacterium pseudotuberculosis phospholipase D gene.h[electronic resource]  c1995  aAbstract: 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.  aBacterial vaccines  aCaseous lymphadenitis  aFormaldehyde  aGene expression  aGenetic resistance  aImmunology  aPhospholipase D  aSheep  aToxins  aLinfadenite Caseosa  aToxina  aVacina  aBase Sequence  aExpressão genética  aFosfolipase  aGenetic toxoid  aInativacao gene  aMolecular Sequence Data1 aKRYWULT, J.1 aMOORE, R. J.1 aHODGON, A. L. M.  tVaccinegv. 13, n. 18, p. 1785-1792, Dec. 1995.