| 2016 |
MYR1 (TGGT1_254470) is a secreted protein that is cleaved by TgASP5 into two stable fragments, both of which localize within the parasitophorous vacuole (PV) and at the parasitophorous vacuole membrane (PVM). Deletion of MYR1 abolishes GRA24 transit to the host nucleus, establishing MYR1 as essential machinery for translocation of dense granule effectors (including GRA16 and GRA24) from the PV into the host cell cytosol and nucleus. MYR1 is also required for host c-Myc upregulation. |
Whole-genome sequencing of flow-cytometry-selected mutants; immunofluorescence localization; genetic deletion (ΔMyR1) with host c-Myc and GRA24 nuclear transit as phenotypic readouts; TgASP5-dependent cleavage assay |
mBio |
High |
26838724
|
| 2018 |
MYR1 forms a protein complex at the PVM with MYR2 and MYR3. MYR2 and MYR3 are secreted into the PV space and co-localize with PVM and MYR1. MYR3, but not MYR2, stably associates with MYR1. The N- and C-terminal fragments of MYR1 are disulfide-linked. All three proteins are membrane-associated (consistent with predicted transmembrane domains). MYR2 and MYR3 are required for translocation of a subset of GRAs (GRA16, GRA24) into the host cell. |
Co-immunoprecipitation; immunofluorescence co-localization; genetic screens (c-Myc and GRA export assays in mutants); DHFR domain fusion block-of-function assay supporting a translocon model |
PLoS pathogens |
High |
29357375
|
| 2018 |
RNA-Seq of human foreskin fibroblasts infected with RHΔmyr1 vs. wild-type established that the majority of differentially regulated host genes responding to Toxoplasma infection are MYR1-dependent. A subset of MYR1-dependent responses are ASP5-independent, indicating MYR1 function does not strictly require ASP5 cleavage for export of some effectors. MYR1-dependent effects include upregulation of E2F transcription factors/cell cycle genes and downregulation of interferon signaling. |
RNA-Seq transcriptomics of infected host cells; genetic deletion of MYR1 and ASP5 compared to wild-type |
mBio |
Medium |
29615509
|
| 2019 |
ROP17, a rhoptry serine/threonine protein kinase, is required for MYR1-dependent translocation of dense granule effectors across the PVM. Null or catalytically dead ROP17 mutants are defective in GRA translocation. ROP17 acts from the host cytosolic side of the PVM (trans-rescue by ROP17 from co-infecting parasites rescues translocation), placing it as a component upstream of or parallel to the MYR translocon complex. |
Whole-genome sequencing of translocation-defective mutants; genetic complementation and trans-rescue experiments; catalytic dead mutant construction; immunofluorescence |
mSphere |
High |
31366709
|
| 2019 |
HCE1, a novel dense granule effector, is exported from the PV in a MYR1-dependent manner and localizes to the host nucleus, where it binds E2F3, E2F4, and DP1 transcription factors (shown by immunoprecipitation from infected host cells) and is necessary and sufficient to upregulate cyclin E and E2F target genes. |
Genetic deletion (ΔHce1); immunoprecipitation from infected host cells; expression in uninfected HFFs and Neospora caninum for sufficiency; immunofluorescence |
mBio |
High |
31040242
|
| 2020 |
Affinity purification of MYR1 identified interacting proteins MYR4 (TGGT1_211460), GRA54 (TGGT1_204340), PPM3C (TGGT1_270320), GRA44, and GRA45 within the PV. Of these, GRA44, GRA45, and MYR4 are each essential for GRA16 translocation and host c-Myc/cyclin E1 upregulation, expanding the translocon complex to at least eight discrete proteins. |
Affinity purification/Co-immunoprecipitation of MYR1 followed by mass spectrometry; genetic deletion of identified interactors with GRA16 translocation and c-Myc/cyclin E1 as functional readouts |
mSphere |
High |
32075880
|
| 2020 |
GRA44, which contains a putative acid phosphatase domain, physically interacts with MYR1 (shown by immunoprecipitation) and is required for host cell c-Myc upregulation downstream of effector secretion, phenocopying loss of the MYR translocon. |
Immunoprecipitation; conditional knockdown of GRA44; c-Myc upregulation assay |
mSphere |
Medium |
32075881
|
| 2020 |
MYR1 is identified as a component of the cyst wall proteome in vitro. During tachyzoite-to-bradyzoite transition, the export of effectors (GRA16, GRA24, TgIST, and others) into the host nucleus occurs primarily during early time points post-infection, with diminishing nuclear accumulation at later stages. TgIST-mediated suppression of IFN-γ signaling persists in bradyzoite infection, demonstrating continued functional effector export beyond early stages. |
Epitope tagging of endogenous effector loci; immunofluorescence assays at multiple time points during bradyzoite differentiation; quantification of host nuclear accumulation |
mBio |
Medium |
32156805
|
| 2020 |
TgPPM3C, a PP2C-class serine/threonine phosphatase that co-immunoprecipitates with MYR1, is required for export of GRA16 and GRA28 but not other MYR1-dependent effectors. Phosphoproteomic analysis shows that loss of PPM3C alters phosphorylation of GRA16, GRA28, and MYR1 itself. Phosphomimetic mutation of two GRA16 serine residues causes export defects, indicating that de-phosphorylation by PPM3C is a prerequisite for GRA16 export through the MYR translocon. |
Genetic deletion of PPM3C; phosphoproteomics; phosphomimetic mutagenesis of GRA16; immunofluorescence for effector nuclear localization; prior Co-IP establishing MYR1 interaction (PMID:32075880) |
PLoS pathogens |
High |
33370417
|
| 2020 |
Single-cell transcriptomic analysis of uninfected-injected (U-I) cells versus infected cells from wild-type and ΔMyR1 parasites established that the host's earliest transcriptional response to infection is driven primarily by injected ROPs, not MYR1-dependent GRAs. MYR1-dependent GRA effectors counter-act ROP-driven pro-inflammatory signatures, and MYR1-dependent paracrine effects further modulate inflammatory responses in bystander cells. |
Single-cell RNA-Seq of flow-sorted U-I, infected, and uninfected cells; genetic deletion of MYR1 |
mBio |
Medium |
32518180
|
| 2021 |
In bradyzoites, MYR1-dependent protein export is responsible for transcriptional remodeling of host cells, including suppression of type I IFN and IFN-γ signaling pathways. Loss of MYR1 abrogates this transcriptional remodeling and removes protection of host cells from IFN-γ-mediated cell death. |
Genetic deletion of MYR1 in bradyzoite stage; RNA-Seq; IFN-γ-mediated cell death assays |
Cell host & microbe |
High |
34921775
|
| 2022 |
GRA28, a dense granule effector, is released from the PV via the MYR1 secretory pathway, traffics to the host cell nucleus, and cooperates with host chromatin remodelers to drive CCR7 expression and chemotactic migration of parasitized macrophages. In vivo, MYR1-deficient parasites are outcompeted in dissemination by wild-type parasites. |
Genetic deletion of MYR1 and GRA28; adoptive transfer in vivo migration assays; immunofluorescence; chromatin remodeler interaction studies |
Cell host & microbe |
High |
36309013
|
| 2022 |
ASP5 is required for proteolytic cleavage of MYR1 and other substrates (GRAs) at an ASPH motif in the Golgi, enabling their proper localization within the PV/PVM and their function in the MYR1/2/3 export translocon. Bradyzoite-stage ASP5 substrates also participate in cyst wall formation. |
N-terminal amine isotopic labeling of substrates (TAILS) to map cleavage sites; genetic deletion of ASP5; comparison of tachyzoite and bradyzoite N-terminomes |
Molecular microbiology |
Medium |
36210525
|
| 2024 |
MYR1 is required for T. gondii-induced early S-phase arrest and double-strand DNA breaks in primary human host cells within 15 min of infection. ΔMyR1 tachyzoites fail to induce S-phase arrest and DNA damage foci. This MYR1-dependent DNA damage is ROS-independent and is not mediated by HCE1/cyclin E1 overexpression. |
Genetic deletion of MYR1 and HCE1; cell cycle analysis; γH2AX foci quantification for DNA damage; ROS inhibitor experiments; time-course immunofluorescence |
Communications biology |
Medium |
39681694
|
| 2024 |
MYR1-dependent secreted proteins generate a permissive host niche in a paracrine manner: wild-type parasites co-infecting the same host can rescue ΔMYR1 parasite growth in vivo, independent of adaptive immunity or key pro-inflammatory cytokines. MYR1 is not required for parasite survival within IFN-γ-activated macrophages, indicating its primary function is paracrine niche creation rather than protection of the infected cell. |
Co-infection experiments in mice with WT and ΔMYR1 parasites; immunodeficient mouse models; cytokine knockout mouse models; in vitro macrophage survival assays |
eLife |
High |
39654402
|
| 2026 |
Activation of the non-canonical NF-κB pathway (nuclear accumulation of RelB and p52) during T. gondii infection is strictly MYR1-dependent. Mechanistically, MYR1-dependent effectors drive depletion of the negative regulator TRAF3, leading to NIK stabilization, p100 phosphorylation, and p52 processing. Eight MYR1-dependent effectors (IST, NSM, HCE1/TEEGR, GRA16, GRA18, GRA24, GRA28, GRA84) function additively through this pathway; no single effector is solely responsible. |
Genetic deletion of MYR1; combinatorial knockout parasites lacking multiple effectors; immunoblot for TRAF3/NIK/p100/p52; immunofluorescence for RelB/p52 nuclear accumulation |
bioRxivpreprint |
Medium |
41959509
|