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Bovine leukosis --- In vitro experimentation --- Pathogenicity --- Vaccines

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Bovine leukaemia virus (BLV) is the etiologic agent of enzootic bovine leukosis. The Tax protein (translated from the X region of the BLV genome) is involved in the long terminal repeat-directed transactivating activity and contributes to the immortalization of primary cells. The aim of this study was the determination of the type of the phosphorylated amino acids, their position in the Tax protein and the influence of Tax protein phosphorylation on its biological activity. It appears that two major phosphorylated sites of the Tax protein are serine 106 and serine 293. The Tax protein phosphorylation is dispensable for the transactivation activity. The calmodulin protein appears to play a key role in Tax phosphorylation. Indeed, antagonist of the calmodulin (W7) inhibits the Tax protein phosphorylation. The serine 106 is phosphorylated in vitro by the PKA, the PKC, the cdc2 kinase and the MAP kinase. The serine 106 thus appears to be an important phosphorylation site in vitro. In contrast, the serine 293 is only phosphorylated by the cdc2- and MAP kinases. However the mutation on serine 106 does not affect the infectious potential of the bovine leukaemia virus.

Bovine leukosis --- Viroses --- Binding proteins --- Phosphorylation

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Bovine leukosis --- viruses. --- viruses --- Vaccines --- Immunization --- Immune response