ArticleJournal of virology1999
Monoclonal antibodies against the minimal DNA-binding domain in the carboxyl-terminal region of human immunodeficiency virus type 1 integrase.
Article in Journal of virology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Multimodal Functionalities of HIV-1 Integrase.Viruses · 2022Review
- Structural dynamics of native and V260E mutant C-terminal domain of HIV-1 integrase.Journal of computer-aided molecular design · 2015Article
- Correlation of recombinant integrase activity and functional preintegration complex formation during acute infection by replication-defective integrase mutant human immunodeficiency virus.Journal of virology · 2012Article
- Cooperation between reverse transcriptase and integrase during reverse transcription and formation of the preintegrative complex of Ty1.Eukaryotic cell · 2006Article
- Role of integrase in reverse transcription of the Saccharomyces cerevisiae retrotransposon Ty1.Eukaryotic cell · 2005Article
- Interaction between human immunodeficiency virus type 1 reverse transcriptase and integrase proteins.Journal of virology · 2004Article
- Replication of chimeric human immunodeficiency virus type 1 (HIV-1) containing HIV-2 integrase (IN): naturally selected mutations in IN augment DNA synthesis.Journal of virology · 2003Article
- Inhibition of the integrases of human immunodeficiency viruses type 1 and type 2 by reverse transcriptases.The Biochemical journal · 2002Article
- Recombinant rabbit single-chain antibodies bind to the catalytic and C-terminal domains of HIV-1 integrase protein and strongly inhibit HIV-1 replication.Biotechnology and applied biochemistryArticle
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Integrase of human immunodeficiency virus type 1 (HIVIN) consists of 288 amino acids, and its minimum DNA-binding domain (MDBD) (amino acids [aa] 220 to 270) is required for the integration reaction. We produced and characterized four murine monoclonal antibodies (MAbs) to the MDBD of HIVIN (strain LAI). Immunoblot and enzyme-linked immunosorbent assays with truncated HIVINs showed that those MAbs recognized sequential epitopes within the MDBD (aa 228 to 236, 237 to 252, 253 to 261, and 262 to 270). Their binding to HIVIN inhibited terminal cleavage and strand transfer activities but not disintegration activity in vitro. This collection of MAbs is useful for studying the structure and function of the MDBD by complementing mutational analyses and other biochemical studies.
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