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. 1997 Dec;71(12):9358–9365. doi: 10.1128/jvi.71.12.9358-9365.1997

Human immunodeficiency virus type 1 Vif protein binds to the Pr55Gag precursor.

M Bouyac 1, M Courcoul 1, G Bertoia 1, Y Baudat 1, D Gabuzda 1, D Blanc 1, N Chazal 1, P Boulanger 1, J Sire 1, R Vigne 1, B Spire 1
PMCID: PMC230239  PMID: 9371595

Abstract

The Vif protein of human immunodeficiency virus type 1 is required for productive replication in peripheral blood lymphocytes. Previous reports suggest that vif-deleted viruses are limited in replication because of a defect in the late steps of the virus life cycle. One of the remaining questions is to determine whether the functional role of Vif involves a specific interaction with virus core proteins. In this study, we demonstrate a direct interaction between Vif and the Pr55Gag precursor in vitro as well as in infected cells. No interaction is observed between Vif and the mature capsid protein. The Pr55Gag-Vif interaction is detected (i) in the glutathione S-transferase system, with in vitro-translated proteins demonstrating a critical role of the NC p7 domain of the Gag precursor; (ii) with proteins expressed in infected cells; and (iii) by coimmunoprecipitation experiments. Deletion of the C-terminal 22 amino acids of Vif abolishes its interaction with the Pr55Gag precursor. Furthermore, point mutations in the C-terminal domain of Vif which have been previously shown to abolish virus infectivity and binding to cell membranes dramatically decrease the Gag-Vif interaction. These results suggest that the interaction between Vif and the pr55Gag precursor is a critical determinant of Vif function.

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Selected References

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