ArticleThe Journal of biological chemistry2012
The GTPase activity of murine guanylate-binding protein 2 (mGBP2) controls the intracellular localization and recruitment to the parasitophorous vacuole of Toxoplasma gondii.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
35 citing papers in PubMed, 58 citations in OpenAlex.
- GBP5-triggered AIM2 inflammasome drives host defense and exacerbates disease severity during Neospora caninum infection.Veterinary research · 2026Article
- Molecular mechanisms and functions of guanylate-binding protein 2 in inflammation and cancer (Review).Oncology letters · 2025Review
- Lymphotoxin beta receptorInfection and immunity · 2025Article
- Utilizing AI for the Identification and Validation of Novel Therapeutic Targets and Repurposed Drugs for Endometriosis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Article
- From mechanisms to therapies: the multifaceted roles of guanylate-binding protein 2 in immunity, cancer, and beyond.Frontiers in immunology · 2025Review
- Evolutionary and functional characterization of lagomorph guanylate-binding proteins: a story of gain and loss and shedding light on expression, localization and innate immunity-related functions.Frontiers in immunology · 2024Article
- Integrative modeling of guanylate binding protein dimers.Protein science : a publication of the Protein Society · 2023Article
- Article
- Domain motions, dimerization, and membrane interactions of the murine guanylate binding protein 2.Scientific reports · 2023Article
- Toxoplasma-proximal and distal control by GBPs in human macrophages.Pathogens and disease · 2022Article
- Murine Irgm Paralogs Regulate Nonredundant Functions To Execute Host Defense to Toxoplasma gondii.Infection and immunity · 2021Article
- Toxoplasma gondii infection and its implications within the central nervous system.Nature reviews. Microbiology · 2021Review
- Targeted Transcriptomic Analysis of C57BL/6 and BALB/c Mice During Progressive ChronicFrontiers in cellular and infection microbiology · 2021Article
- Article
- Guanylate-binding protein 2 orchestrates innate immune responses against murine norovirus and is antagonized by the viral protein NS7.The Journal of biological chemistry · 2020Article
- Article
- Innate, adaptive, and cell-autonomous immunity against Toxoplasma gondii infection.Experimental & molecular medicine · 2019Review
- Human GBP1 is a microbe-specific gatekeeper of macrophage apoptosis and pyroptosis.The EMBO journal · 2019Article
- Interferon-induced guanylate-binding proteins: Guardians of host defense in health and disease.The Journal of experimental medicine · 2019Review
Corrections and comments
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Authors and funding
12 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
One of the most abundantly IFN-γ-induced protein families in different cell types is the 65-kDa guanylate-binding protein family that is recruited to the parasitophorous vacuole of the intracellular parasite Toxoplasma gondii. Here, we elucidate the relationship between biochemistry and cellular host defense functions of mGBP2 in response to Toxoplasma gondii. The wild type protein exhibits low affinities to guanine nucleotides, self-assembles upon GTP binding, forming tetramers in the activated state, and stimulates the GTPase activity in a cooperative manner. The products of the two consecutive hydrolysis reactions are both GDP and GMP. The biochemical characterization of point mutants in the GTP-binding motifs of mGBP2 revealed amino acid residues that decrease the GTPase activity by orders of magnitude and strongly impair nucleotide binding and multimerization ability. Live cell imaging employing multiparameter fluorescence image spectroscopy (MFIS) using a Homo-FRET assay shows that the inducible multimerization of mGBP2 is dependent on a functional GTPase domain. The consistent results indicate that GTP binding, self-assembly, and stimulated hydrolysis activity are required for physiological localization of the protein in infected and uninfected cells. Ultimately, we show that the GTPase domain regulates efficient recruitment to T. gondii in response to IFN-γ.
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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.