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Registro Completo |
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Biblioteca(s): |
Embrapa Caprinos e Ovinos. |
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Data corrente: |
23/05/2000 |
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Data da última atualização: |
03/08/2023 |
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Autoria: |
TACHEDJIAN, M.; KRYWULT, J.; MOORE, R. J.; HODGON, A. L. M. |
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Título: |
Caseous lymphadenitis vaccine development: site-specific inactivation of the Corynebacterium pseudotuberculosis phospholipase D gene. |
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Ano de publicação: |
1995 |
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Fonte/Imprenta: |
Vaccine, v. 13, n. 18, p. 1785-1792, Dec. 1995. |
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DOI: |
10.1016/0264-410x(95)00144-p. |
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Idioma: |
Inglês |
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Conteúdo: |
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. |
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Palavras-Chave: |
Base Sequence; Expressão genética; Fosfolipase; Genetic toxoid; Inativacao gene; Molecular Sequence Data. |
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Thesagro: |
Linfadenite Caseosa; Toxina; Vacina. |
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Thesaurus Nal: |
Bacterial vaccines; Caseous lymphadenitis; Formaldehyde; Gene expression; Genetic resistance; Immunology; Phospholipase D; Sheep; Toxins. |
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Categoria do assunto: |
-- |
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Marc: |
LEADER 02088naa a2200385 a 4500
001 1524117
005 2023-08-03
008 1995 bl uuuu u00u1 u #d
024 7 $a10.1016/0264-410x(95)00144-p.$2DOI
100 1 $aTACHEDJIAN, M.
245 $aCaseous lymphadenitis vaccine development$bsite-specific inactivation of the Corynebacterium pseudotuberculosis phospholipase D gene.$h[electronic resource]
260 $c1995
520 $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.
650 $aBacterial vaccines
650 $aCaseous lymphadenitis
650 $aFormaldehyde
650 $aGene expression
650 $aGenetic resistance
650 $aImmunology
650 $aPhospholipase D
650 $aSheep
650 $aToxins
650 $aLinfadenite Caseosa
650 $aToxina
650 $aVacina
653 $aBase Sequence
653 $aExpressão genética
653 $aFosfolipase
653 $aGenetic toxoid
653 $aInativacao gene
653 $aMolecular Sequence Data
700 1 $aKRYWULT, J.
700 1 $aMOORE, R. J.
700 1 $aHODGON, A. L. M.
773 $tVaccine$gv. 13, n. 18, p. 1785-1792, Dec. 1995.
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Registro original: |
Embrapa Caprinos e Ovinos (CNPC) |
