Purification and partial characterization of human immunodeficiency virus type 2 reverse transcriptase.

A L DeVico; T D Copeland; F D Veronese; S Oroszlan; R C Gallo; M G Sarngadharan

doi:10.1089/aid.1989.5.51

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Purification and partial characterization of human immunodeficiency virus type 2 reverse transcriptase.

A L DeVico·T D Copeland·F D Veronese·S Oroszlan·R C Gallo·M G Sarngadharan

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Abstract

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.

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Amino Acid Sequence Antibodies, Monoclonal Cell Line, Transformed Cross Reactions Endoribonucleases HIV Antibodies HIV-2 Immunoblotting Molecular Sequence Data RNA-Directed DNA Polymerase Ribonuclease H Journal Article Research Support, U.S. Gov't, P.H.S.

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A L DeVico, T D Copeland, F D Veronese, S Oroszlan, R C Gallo, M G Sarngadharan. 1989. Purification and partial characterization of human immunodeficiency virus type 2 reverse transcriptase.. https://doi.org/10.1089/aid.1989.5.51

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