ArticleThe Journal of biological chemistry2015
Microtubule-associated proteins 1 (MAP1) promote human immunodeficiency virus type I (HIV-1) intracytoplasmic routing to the nucleus.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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50 citing papers in PubMed, 73 citations in OpenAlex.
- Bovine coronavirus enters PBIECs via membrane fusion and clathrin-, caveolin-mediated endocytosis, macropinocytosis.Virulence · 2026Article
- Discovery of 4-Quinazolinone-Containing Phenylalanine Derivatives as Potent, Resistant-Tolerant HIV Capsid Inhibitors.MedComm · 2026Article
- Microtubule remodeling by the innate immune factor Trim69 compromises dynein-dependent migration of HIV virion cores toward the nucleus.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Reverse transcription progression and genome length regulate HIV-1 core elasticity and disassembly.PLoS pathogens · 2025Article
- Microtubule acetylation is not required for HIV-1 infection or TRIM69-mediated restriction of HIV-1 infection.Journal of virology · 2025Article
- Review
- TRIM Proteins and Antiviral Microtubule Reorganization: A Novel Component in Innate Immune Responses?Viruses · 2024Review
- The host cytoskeleton: a key regulator of early HIV-1 infection.The FEBS journal · 2024Review
- Capsid-host interactions for HIV-1 ingress.Microbiology and molecular biology reviews : MMBR · 2023Review
- Cellular resistance to an oncolytic virus is driven by chronic activation of innate immunity.iScience · 2023Article
- Review
- Unraveling the Dynamic Role of Microtubules in the HBV Life Cycle.Journal of clinical and translational hepatology · 2022Article
- Hepatitis B Virus Induces Microtubule Stabilization to Promote Productive Infection through Upregulating Microtubule-associated Protein 1S.Journal of clinical and translational hepatology · 2022Article
- HIV-1 Accessory Proteins Impart a Modest Interferon Response and Upregulate Cell Cycle-Related Genes in Macrophages.Pathogens (Basel, Switzerland) · 2022Article
- Identification of immuno-infiltrating MAP1A as a prognosis-related biomarker for bladder cancer and its ceRNA network construction.Frontiers in oncology · 2022Article
- Rotten to the core: antivirals targeting the HIV-1 capsid core.Retrovirology · 2021Review
- Nuclear Import of HIV-1.Viruses · 2021Review
- Repurposing Cardiac Glycosides: Drugs for Heart Failure Surmounting Viruses.Molecules (Basel, Switzerland) · 2021Review
- The Role of Capsid in HIV-1 Nuclear Entry.Viruses · 2021Review
- HIV-1 capsid exploitation of the host microtubule cytoskeleton during early infection.Retrovirology · 2021Review
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Authors and funding
13 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
After cell entry, HIV undergoes rapid transport toward the nucleus using microtubules and microfilaments. Neither the cellular cytoplasmic components nor the viral proteins that interact to mediate transport have yet been identified. Using a yeast two-hybrid screen, we identified four cytoskeletal components as putative interaction partners for HIV-1 p24 capsid protein: MAP1A, MAP1S, CKAP1, and WIRE. Depletion of MAP1A/MAP1S in indicator cell lines and primary human macrophages led to a profound reduction in HIV-1 infectivity as a result of impaired retrograde trafficking, demonstrated by a characteristic accumulation of capsids away from the nuclear membrane, and an overall defect in nuclear import. MAP1A/MAP1S did not impact microtubule network integrity or cell morphology but contributed to microtubule stabilization, which was shown previously to facilitate infection. In addition, we found that MAP1 proteins interact with HIV-1 cores both in vitro and in infected cells and that interaction involves MAP1 light chain LC2. Depletion of MAP1 proteins reduced the association of HIV-1 capsids with both dynamic and stable microtubules, suggesting that MAP1 proteins help tether incoming viral capsids to the microtubular network, thus promoting cytoplasmic trafficking. This work shows for the first time that following entry into target cells, HIV-1 interacts with the cytoskeleton via its p24 capsid protein. Moreover, our results support a role for MAP1 proteins in promoting efficient retrograde trafficking of HIV-1 by stimulating the formation of stable microtubules and mediating the association of HIV-1 cores with microtubules.
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