ArticleJournal of virology2015
Contribution of MxB oligomerization to HIV-1 capsid binding and restriction.
Article in Journal of virology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
36 citing papers in PubMed, 51 citations in OpenAlex.
- Interferon-induced MXB protein restricts vimentin-dependent viral infection.Acta pharmaceutica Sinica. B · 2024Article
- Capsid-host interactions for HIV-1 ingress.Microbiology and molecular biology reviews : MMBR · 2023Review
- Review
- MX2 Viral Substrate Breadth and Inhibitory Activity Are Regulated by Protein Phosphorylation.mBio · 2022Article
- Clade-Specific Alterations within the HIV-1 Capsid Protein with Implications for Nuclear Translocation.Biomolecules · 2022Article
- The interferon-inducible GTPase MxB promotes capsid disassembly and genome release of herpesviruses.eLife · 2022Article
- Selection and identification of an RNA aptamer that specifically binds the HIV-1 capsid lattice and inhibits viral replication.Nucleic acids research · 2022Article
- MxB inhibits long interspersed element type 1 retrotransposition.PLoS genetics · 2022Article
- MX2-mediated innate immunity against HIV-1 is regulated by serine phosphorylation.Nature microbiology · 2021Article
- Review
- GTPase Activity of MxB Contributes to Its Nuclear Location, Interaction with Nucleoporins and Anti-HIV-1 Activity.Virologica Sinica · 2021Article
- Structure, Function, and Interactions of the HIV-1 Capsid Protein.Life (Basel, Switzerland) · 2021Review
- HIV-1 resists MxB inhibition of viral Rev protein.Emerging microbes & infections · 2020Article
- Article
- MxB impedes the NUP358-mediated HIV-1 pre-integration complex nuclear import and viral replication cooperatively with CPSF6.Retrovirology · 2020Article
- Article
- Pro-515 of the dynamin-like GTPase MxB contributes to HIV-1 inhibition by regulating MxB oligomerization and binding to HIV-1 capsid.The Journal of biological chemistry · 2020Article
- MX 2 is a novel regulator of cell cycle in melanoma cells.Pigment cell & melanoma research · 2020Article
- The anti-viral dynamin family member MxB participates in mitochondrial integrity.Nature communications · 2020Article
- Methadone Inhibits Viral Restriction Factors and Facilitates HIV Infection in Macrophages.Frontiers in immunology · 2020Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
unlabelledThe alpha interferon (IFN-α)-inducible restriction factor myxovirus B (MxB) blocks HIV-1 infection after reverse transcription but prior to integration. MxB binds to the HIV-1 core, which is composed of capsid protein, and this interaction leads to inhibition of the uncoating process of HIV-1. Previous studies suggested that HIV-1 restriction by MxB requires binding to capsid. This work tests the hypothesis that MxB oligomerization is important for the ability of MxB to bind to the HIV-1 core. For this purpose, we modeled the structure of MxB using the published tertiary structure of MxA. The modeled structure of MxB guided our mutagenic studies and led to the discovery of several MxB variants that lose the capacity to oligomerize. In agreement with our hypothesis, MxB variants that lost the oligomerization capacity also lost the ability to bind to the HIV-1 core. MxB variants deficient for oligomerization were not able to block HIV-1 infection. Overall, our work showed that oligomerization is required for the ability of MxB to bind to the HIV-1 core and block HIV-1 infection. IMPORTANCE: MxB is a novel restriction factor that blocks infection of HIV-1. MxB is inducible by IFN-α, particularly in T cells. The current work studies the oligomerization determinants of MxB and carefully explores the contribution of oligomerization to capsid binding and restriction. This work takes advantage of the current structure of MxA and models the structure of MxB, which is used to guide structure-function studies. This work leads to the conclusion that MxB oligomerization is important for HIV-1 capsid binding and restriction.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.