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11th International AIDS ConferenceVancouver, British Columbia — July 7-12, 1996 |
Int Conf AIDS 1996 Jul 7-12; 11:18 (abstract no. Th.A.925)
Cartier C, Deckert M, Grangeasse C, Trauger R, Jensen F, Bernard A, Cozzone A, Desgranges C, Boyer V; INSERM, Lyon, France. Fax: 33/72 68 19 71. E-mail: boyer@lyon151.inserm.fr.
OBJECTIVE: To determine if a protein kinase activity would be associated with HIV-1 viral particles.
METHODS: In vitro phosphorylation assays were performed with viral particles purified through chromatography in presence of gamma32P-ATP to demonstrate the presence of a kinase activity. Bidimensional gel electrophoresis and blotting of the radiophosphorylated virus were realized in order to superimpose the phosphorylation pattern and the reactivity against anti-viral and anti-cellular protein antibodies.
RESULTS: We observed phosphorylation of viral and cellular proteins associated with the virus by an endogenous protein kinase activity. These findings are reproducible with two different viral strains obtained from two CD4+ cell lines. The phosphoamino acid analysis revealed phosphorylated serine and threonine residues. In addition, in-gel assay experiments showed the phosphorylation of three protein kinases. Further characterizations revealed the presence of the ERK2 MAPK (Mitogen-Activated Protein Kinase) and the phosphorylation of the viral capsid (CA, p24).
CONCLUSIONS: We demonstrate the presence of virion-associated protein kinases, which phosphorylate cellular and viral proteins. Future studies will be necessary to clarify the function of these protein kinases during viral replication.
960707
ThA925
Copyright © 1996 - International AIDS Society (IAS). Reproduction of this abstract (other than one copy for personal reference) must be cleared through the IAS.