In ∼ 10% of natural human immunodeficiency virus 1 (HIV-1) gene populations, sequences of shortened open reading frames with premature stop codons have been found. Here we report the functional analysis of two patient-derived genes. 45-2 encodes a C terminally truncated Vif protein of only 173 instead of 192 amino acids and additionally contains several rare amino acid substitutions which are in part shared by A65-5. HIV-1 pNL4-3-derived recombinant A45-2 and A65-5 virions were fully infectious in H9 cells and human PBMC, both known to be non-permissive for -defective HIV-1. Furthermore, A45-2 virions produced in primary human monocyte-derived macro-phages were infectious for MT-4 cells. This study unequivocally demonstrates that the C-terminal region (19 amino acids) of the Vif protein is dispensable for Vif function in the cell culture systems employed. Additionally, we investigated whether the Vif protein might be phosphorylated and obtained no evidence for this.


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