Isolation and characterization of a novel protein (X-ORF product) from SIV and HIV-2.

Abstract

A protein designated p14 was purified from a simian immunodeficiency virus (SIVMne) and was shown by amino acid sequence analysis to be nearly identical to the predicted translational product of a unique open reading frame (X-ORF) in the nucleotide sequences of SIVmac and human immunodeficiency virus type 2 (HIV-2). Thus the X-ORF is proven to be a new retroviral gene. The p14 is present in SIVMne in molar amounts equivalent to those of the gag proteins. This is the first example of a retrovirus that contains a substantial quantity of a viral protein that is not a product of the gag, pro, pol, or env genes. SIV p14 and its homolog in HIV-2 may function as nucleic acid binding proteins since purified p14 binds to single-stranded nucleic acids in vitro. Antisera to the purified protein detected p14 in SIVMne, SIVmac, and a homologous protein (16 kilodaltons) in HIV-2 but did not react with HIV-1. Diagnostic procedures based on this novel protein will distinguish between HIV-1 and HIV-2.

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@article{Henderson1988IsolationAC, title={Isolation and characterization of a novel protein (X-ORF product) from SIV and HIV-2.}, author={Louis E. Henderson and Raymond C. Sowder and Terry D. Copeland and Raoul E. Benveniste and Stephen Oroszlan}, journal={Science}, year={1988}, volume={241 4862}, pages={199-201} }