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

Purification and partial characterization of human immunodeficiency virus type 2 reverse... 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png AIDS research and human retroviruses Pubmed

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

DeVico, A L; Copeland, T D; Veronese, F D; Oroszlan, S; Gallo, R C; Sarngadharan, M G
AIDS research and human retroviruses , Volume 5 (1): 10 – Jul 3, 1989
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Purification and partial characterization of human immunodeficiency virus type 2 reverse transcriptase.


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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ISSN
0889-2229
DOI
10.1089/aid.1989.5.51
pmid
2470399

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.

Journal

AIDS research and human retroviruses – Pubmed

Published: Jul 3, 1989

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