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- W2100032808 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." @default.
- W2100032808 created "2016-06-24" @default.
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- W2100032808 date "1997-12-01" @default.
- W2100032808 modified "2023-09-26" @default.
- W2100032808 title "Human immunodeficiency virus type 1 Vif protein binds to the Pr55Gag precursor" @default.
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- W2100032808 doi "https://doi.org/10.1128/jvi.71.12.9358-9365.1997" @default.
- W2100032808 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/230239" @default.
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