Isolation and Characterization of a Novel Protein (X-ORF Product) from SIV and HIV-2

• Published in: Science (American Association for the Advancement of Science) Vol. 241; no. 4862; pp. 199 - 201
• Main Authors: Henderson, L. E., Sowder, R. C., T. D Copeland, Benveniste, R. E., Oroszlan, S.
• Format: Journal Article
• Language: English
• Published: Washington, DC The American Association for the Advancement of Science 08.07.1988; American Association for the Advancement of Science
• Subjects: Acquired immune deficiency syndrome; AIDS; AIDS/HIV; Amino Acid Sequence; Amino acids; Biological and medical sciences; DNA-binding protein; Fundamental and applied biological sciences. Psychology; Gels; Growth rings; HIV 1; HIV 2; human immunodeficiency virus 2; Medical research; Microbiology; Molecular Sequence Data; Molecular Weight; Morphology, structure, chemical composition, physicochemical properties; Nucleic acids; Nucleotide sequences; Open reading frames; Peptide Fragments - analysis; Proteins; Retroviridae; Retroviridae Proteins - isolation & purification; simian immunodeficiency virus; Viral proteins; Virology; Viruses; Virus; Characterization; Proteins; Retroviridae; Isolation; Chemical composition; Human immunodeficiency virus; Simian immunodeficiency virus
• ISSN: 0036-8075; 1095-9203
• DOI: 10.1126/science.3388031

A protein designated p14 was purified from a simian immunodeficiency virus (SIV$_{\text{Mne}}$) 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 SIV$_{\text{mac}}$ 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 SIV$_{\text{Mne}}$ 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 SIV$_{\text{Mne}}$, SIV$_{\text{mac}}$, 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.