Purification and partial characterization of human immunodeficiency virus type 2 reverse transcriptase.
We have raised a rabbit monospecific antibody against a synthetic peptide derived from a sequence within the COOH-terminal portion of the reverse transcriptase (RT) of HIV-1. This sequence was also found to be conserved in the predicted amino acid sequence of HIV-2. The antibody, designated C2003, cross-reacted with HIV-2 RT on immunoblots of HIV-2 virus extract and directly inhibited HIV-2 RT activity. Fractionation of HIV-2 RT by immunoaffinity chromatography with C2003 antibody yielded a pair of viral proteins of 68 and 55 kD associated with both RT and RNAse H activities. Both proteins were found to be highly immunogenic, recognized by 11 of 11 human sera that previously tested positive for antibodies to HIV-2 antigens in immunoblot assays.
DeVico
A L
AL
Department of Cell Biology, Bionetics Research, Inc., Rockville, MD 20850.
Copeland
T D
TD
Veronese
F D
FD
Oroszlan
S
S
Gallo
R C
RC
Sarngadharan
M G
MG
D000595:Amino Acid Sequence; D000911:Antibodies, Monoclonal / Q000276:immunology; D002461:Cell Line, Transformed; D003429:Cross Reactions; D004722:Endoribonucleases / Q000302:isolation & purification; D015483:HIV Antibodies / Q000276:immunology*; D015498:HIV-2 / Q000201:enzymology* / Q000276:immunology; D015151:Immunoblotting; D008969:Molecular Sequence Data; D012194:RNA-Directed DNA Polymerase / Q000302:isolation & purification*; D016914:Ribonuclease H
D000911:Antibodies, Monoclonal; D015483:HIV Antibodies; D012194:RNA-Directed DNA Polymerase; D004722:Endoribonucleases; D016914:Ribonuclease H