Isolation and characterization of a novel protein (X-ORF product) from SIV and HIV-2.
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.
Henderson
L E
LE
Bionetics Research, Inc., National Cancer Institute, Frederick, MD 21701.
Sowder
R C
RC
Copeland
T D
TD
Benveniste
R E
RE
Oroszlan
S
S
D000595:Amino Acid Sequence; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D012190:Retroviridae; D012191:Retroviridae Proteins / Q000302:isolation & purification*
D010446:Peptide Fragments; D012191:Retroviridae Proteins