Non-Catalytic Site HIV-1 Integrase Inhibitors Disrupt Core Maturation and Induce a Reverse Transcription Block in Target Cells
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HIV-1 integrase (IN) is the target for two classes of antiretrovirals: i) the integrase strand-transfer inhibitors (INSTIs) and ii) the non-catalytic site integrase inhibitors (NCINIs). NCINIs bind at the IN dimer interface and are thought to interfere primarily with viral DNA (vDNA) integration in the target cell by blocking IN-vDNA assembly as well as the IN-LEDGF/p75 interaction. Herein we show that treatment of virus-producing cells, but not of mature virions or target cells, drives NCINI antiviral potency. NCINIs target an essential late-stage event in HIV replication that is insensitive to LEDGF levels in the producer cells. Virus particles produced in the presence of NCINIs displayed normal Gag-Pol processing and endogenous reverse transcriptase activity, but were defective at initiating vDNA synthesis following entry into the target cell. NCINI-resistant virus carrying a T174I mutation in the IN dimer interface was less sensitive to the compound-induced late-stage effects, including the reverse transcription block. Wild-type, but not T174I virus, produced in the presence of NCINIs exhibited striking defects in core morphology and an increased level of IN oligomers that was not observed upon treatment of mature cell-free particles. Collectively, these results reveal that NCINIs act through a novel mechanism that is unrelated to the previously observed inhibition of IN activity or IN-LEDGF interaction, and instead involves the disruption of an IN function during HIV-1 core maturation and assembly.
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Class II integrase mutations alter viral particle morphology, with ribonucleoprotein material outside the capsid shell, often associated with the viral membrane.
“Class II IN mutations additionally affected viral particle morphology, with the ribonucleoprotein material found outside of the capsid shell, oftentimes in association with the viral membrane131,132,139–142.”
From Structure and function of retroviral integrase (2022) · cites this paper as [142]
The Results section, “Virion Core Morphology is Affected by NCINIs” (page unavailable), reports RNP-like material outside the capsid shell in NCINI-treated particles and independently confirms that phenotype in virus lacking integrase. The Discussion mentions class II integrase mutants in connection with a reverse-transcription block, but our copy does not establish the stated morphology for those mutants or say that the material is associated with the viral membrane. (LLM, conf=0.82)
Experimental — accuracy not yet measuredVirus particles produced in the presence of ALLINIs incorporate viral RNA and proteins properly, but integrase-RNA binding is disrupted and the ribonucleoprotein complex is eccentric.
“Detailed analysis of virus particles produced in the presence of ALLINIs revealed that although viral RNA and proteins were incorporated properly, IN-RNA binding was disrupted, and the ribonucleoprotein complex was located eccentrically (Fig. 6B)140–142,174–176.”
From Structure and function of retroviral integrase (2022) · cites this paper as [142]
The Discussion (page unavailable) says NCINI-produced particles appear normal in genomic RNA and major viral-protein content, while electron microscopy shows the ribonucleoprotein complex mislocalized outside the capsid shell. It does not report that integrase–RNA binding was disrupted; the paper instead reports increased integrase oligomerization. It also qualifies the content finding because a detailed proteomic analysis was not performed. (LLM, conf=0.88)
Experimental — accuracy not yet measuredALLINIs do not act by inhibiting integration.
“Counterintuitively, the underlying mode of ALLINI action is not via inhibition of integration140,142,174–177,179–181.”
From Structure and function of retroviral integrase (2022) · cites this paper as [142]
The Introduction and Discussion say that NCINIs’ primary antiviral effect occurs during virus production, through disrupted core maturation, rather than through inhibition of integration. But the Results also show that GS-B blocks integration when applied to target cells at high concentrations. The categorical claim that ALLINIs do not act by inhibiting integration therefore overstates the paper’s finding. (LLM, conf=0.91)
Experimental — accuracy not yet measuredThe common biochemical consequence of ALLINI binding is aberrant HIV-1 integrase hyper-multimerization.
“The common biochemical consequence of ALLINI binding is aberrant HIV-1 IN hyper-multimerization140,142,174–181.”
From Structure and function of retroviral integrase (2022) · cites this paper as [142]
HIV-1 is more susceptible to ALLINIs when exposed during egress than during ingress.
“Under these conditions, it became clear that HIV-1 was more susceptible to ALLINIs when exposed to the compounds during egress as compared to ingress140,142,174–176.”
From Structure and function of retroviral integrase (2022) · cites this paper as [142]
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- Authors
- Balakrishnan, M., Yant, S. R., Tsai, L., O’Sullivan, C., Bam, R. A., Tsai, A., Niedziela-Majka, A., Stray, K. M., Sakowicz, R., & Cihlar, T.
- Affiliations
- Gilead Sciences (United States) (US)
- Corresponding author
- Balakrishnan, Mini
- Venue
- PLoS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2013-09-09
- Volume
- 8
- Issue
- 9
- Pages
- e74163
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC3767657
- OpenAlex
- W2053936754
- Cited by
- 126
- References
- 54
- Citations by year
- 2026: 4 · 2025: 5 · 2024: 4 · 2023: 6 · 2022: 11 · 2021: 12 · 2020: 12 · 2019: 9 · 2018: 9 · 2017: 7 · 2016: 17 · 2015: 9 · 2014: 17 · 2013: 4
- FWCI
- 11.92
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- PLoS ONE (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, other-oa)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Figshare (submittedVersion, cc-by)
- Topics
- Health Sciences › Medicine › Infectious Diseases › HIV/AIDS drug development and treatment
- Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Virus-based gene therapy research
- Keywords
- HIV-1 integrase, integrase strand transfer inhibitors, LEDGF/p75, viral DNA replication
- MeSH terms
- DNA, Viral, Genetic Vectors, Humans, Luciferases, Mutation, T-Lymphocytes, Transcription Factors, Virion, Virus Replication, HIV-1, Gene Expression, Virus Integration, Genes, Reporter, Virus Assembly, HIV Integrase, HIV Integrase Inhibitors, Drug Resistance, Viral, Cell Line, Tumor, Adaptor Proteins, Signal Transducing, HIV Reverse Transcriptase, Host-Pathogen Interactions
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