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J Biol Chem, Vol. 274, Issue 27, 19434-19440, July 2, 1999

Identification of Three Major Phosphorylation Sites within HIV-1 Capsid
ROLE OF PHOSPHORYLATION DURING THE EARLY STEPS OF INFECTION

Christine Cartier, Peggy Sivard, Corinne Tranchat, Didier Decimo^¶, Claude Desgranges, and Véronique Boyer

From  Virus des Hépatites, Rétrovirus Humains et Pathologies Associées, INSERM U271, 151 Cours. A. Thomas, 69 424 Lyon Cedex 03, France and the ^¶ LaboRetro, Unité de Virologie Humaine, INSERM U412, Ecole Normale Supérieure de Lyon, 46 allée d'Italie, 69 364 Lyon Cedex 07, France

We previously reported the presence of two cellular serine/threonine protein kinases incorporated in human immunodeficiency virus type 1 (HIV-1) particles. One protein kinase is MAPK ERK2 (mitogen-activated protein kinase), whereas the other one, a 53-kDa protein, still needs to be identified. Furthermore, we demonstrated that the capsid protein CAp24 is phosphorylated by one of those two virion-associated protein kinases (Cartier, C., Deckert, M., Grangeasse, C., Trauger, R., Jensen, F., Bernard, A., Cozzone, A., Desgranges, C., and Boyer, V. (1997) J. Virol. 71, 4832-4837). In this study, we showed that CAp24 is not a direct substrate of MAPK ERK2. Moreover, using site-directed mutagenesis of each of the 9 serine residues of CAp24, we demonstrated the phosphorylation of 3 serine residues (Ser-109, Ser-149, and Ser-178) in the CAp24. Substitution of each serine residue did not affect viral budding, nor viral structure. By contrast, substitution of Ser-109, Ser-149, or Ser-178 affects viral infectivity by preventing the reverse transcription process to be completely achieved. Our results suggest that CAp24 serine phosphorylation is essential for viral uncoating process.

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