ArticleNucleic acids research2014
Integrase residues that determine nucleotide preferences at sites of HIV-1 integration: implications for the mechanism of target DNA binding.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed, 63 citations in OpenAlex.
- Core nucleosomes are refractory to lentiviral DNA integration.Nature communications · 2026Article
- Molecular basis for the regulation of retroviral nucleosomal integration by chromatin compaction.Nucleic acids research · 2026Article
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- Dynamic modulation of the non-canonical NF-κB signaling pathway for HIV shock and kill.Frontiers in cellular and infection microbiology · 2024Review
- Unraveling the palindromic and nonpalindromic motifs of retroviral integration site sequences by statistical mixture models.Genome research · 2023Article
- HIV-1 Preintegration Complex Preferentially Integrates the Viral DNA into Nucleosomes Containing Trimethylated Histone 3-Lysine 36 Modification and Flanking Linker DNA.Journal of virology · 2022Article
- Review
- Engineered Sleeping Beauty transposase redirects transposon integration away from genes.Nucleic acids research · 2022Article
- Structure and function of retroviral integrase.Nature reviews. Microbiology · 2022Review
- Modulation of the intrinsic chromatin binding property of HIV-1 integrase by LEDGF/p75.Nucleic acids research · 2021Article
- Investigating site-selection mechanisms of retroviral integration in supercoiled DNA braids.Journal of the Royal Society, Interface · 2021Article
- Integration in oncogenes plays only a minor role in determining the in vivo distribution of HIV integration sites before or during suppressive antiretroviral therapy.PLoS pathogens · 2021Article
- Factors that mold the nuclear landscape of HIV-1 integration.Nucleic acids research · 2021Review
- Retroviral integrase: Structure, mechanism, and inhibition.The Enzymes · 2021Article
- Integrating transposable elements in the 3D genome.Mobile DNA · 2020Article
- Multifaceted HIV integrase functionalities and therapeutic strategies for their inhibition.The Journal of biological chemistry · 2019Review
- Review
- Local features determine Ty3 targeting frequency at RNA polymerase III transcription start sites.Genome research · 2019Article
- Human H4 tail stimulates HIV-1 integration through binding to the carboxy-terminal domain of integrase.Nucleic acids research · 2019Article
- Cat and Mouse: HIV Transcription in Latency, Immune Evasion and Cure/Remission Strategies.Viruses · 2019Review
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Retroviruses favor target-DNA (tDNA) distortion and particular bases at sites of integration, but the mechanism underlying HIV-1 selectivity is unknown. Crystal structures revealed a network of prototype foamy virus (PFV) integrase residues that distort tDNA: Ala188 and Arg329 interact with tDNA bases, while Arg362 contacts the phosphodiester backbone. HIV-1 integrase residues Ser119, Arg231, and Lys258 were identified here as analogs of PFV integrase residues Ala188, Arg329 and Arg362, respectively. Thirteen integrase mutations were analyzed for effects on integrase activity in vitro and during virus infection, yielding a total of 1610 unique HIV-1 integration sites. Purine (R)/pyrimidine (Y) dinucleotide sequence analysis revealed HIV-1 prefers the tDNA signature (0)RYXRY(4), which accordingly favors overlapping flexible dinucleotides at the center of the integration site. Consistent with roles for Arg231 and Lys258 in sequence specific and non-specific binding, respectively, the R231E mutation altered integration site nucleotide preferences while K258E had no effect. S119A and S119T integrase mutations significantly altered base preferences at positions -3 and 7 from the site of viral DNA joining. The S119A preference moreover mimicked wild-type PFV selectivity at these positions. We conclude that HIV-1 IN residue Ser119 and PFV IN residue Ala188 contact analogous tDNA bases to effect virus integration.
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