@article{15276,
  abstract     = {Biotrophic plant pathogens secrete effector proteins to manipulate the host physiology. Effectors suppress defenses and induce an environment favorable to disease development. Sequence-based prediction of effector function is impeded by their rapid evolution rate. In the maize pathogen <jats:italic>Ustilago maydis</jats:italic>, effector-coding genes frequently organize in clusters. Here we describe the functional characterization of the <jats:italic>pleiades</jats:italic>, a cluster of ten effector genes, by analyzing the micro- and macroscopic phenotype of the cluster deletion and expressing these proteins <jats:italic>in planta</jats:italic>. Deletion of the <jats:italic>pleiades</jats:italic> leads to strongly impaired virulence and accumulation of reactive oxygen species (ROS) in infected tissue. Eight of the Pleiades suppress the production of ROS upon perception of pathogen associated molecular patterns (PAMPs). Although functionally redundant, the Pleiades target different host components. The paralogs Taygeta1 and Merope1 suppress ROS production in either the cytoplasm or nucleus, respectively. Merope1 targets and promotes the auto-ubiquitination activity of RFI2, a conserved family of E3 ligases that regulates the production of PAMP-triggered ROS burst in plants.},
  author       = {Navarrete, Fernando and Grujic, Nenad and Stirnberg, Alexandra and Saado, Indira and Aleksza, David and Gallei, Michelle C and Adi, Hazem and Alcântara, André and Khan, Mamoona and Bindics, Janos and Trujillo, Marco and Djamei, Armin},
  issn         = {1553-7374},
  journal      = {PLOS Pathogens},
  keywords     = {Virology, Genetics, Molecular Biology, Immunology, Microbiology, Parasitology},
  number       = {6},
  publisher    = {Public Library of Science},
  title        = {{The Pleiades are a cluster of fungal effectors that inhibit host defenses}},
  doi          = {10.1371/journal.ppat.1009641},
  volume       = {17},
  year         = {2021},
}

@article{7464,
  abstract     = {Retrovirus assembly is driven by the multidomain structural protein Gag. Interactions between the capsid domains (CA) of Gag result in Gag multimerization, leading to an immature virus particle that is formed by a protein lattice based on dimeric, trimeric, and hexameric protein contacts. Among retroviruses the inter- and intra-hexamer contacts differ, especially in the N-terminal sub-domain of CA (CANTD). For HIV-1 the cellular molecule inositol hexakisphosphate (IP6) interacts with and stabilizes the immature hexamer, and is required for production of infectious virus particles. We have used in vitro assembly, cryo-electron tomography and subtomogram averaging, atomistic molecular dynamics simulations and mutational analyses to study the HIV-related lentivirus equine infectious anemia virus (EIAV). In particular, we sought to understand the structural conservation of the immature lentivirus lattice and the role of IP6 in EIAV assembly. Similar to HIV-1, IP6 strongly promoted in vitro assembly of EIAV Gag proteins into virus-like particles (VLPs), which took three morphologically highly distinct forms: narrow tubes, wide tubes, and spheres. Structural characterization of these VLPs to sub-4Å resolution unexpectedly showed that all three morphologies are based on an immature lattice with preserved key structural components, highlighting the structural versatility of CA to form immature assemblies. A direct comparison between EIAV and HIV revealed that both lentiviruses maintain similar immature interfaces, which are established by both conserved and non-conserved residues. In both EIAV and HIV-1, IP6 regulates immature assembly via conserved lysine residues within the CACTD and SP. Lastly, we demonstrate that IP6 stimulates in vitro assembly of immature particles of several other retroviruses in the lentivirus genus, suggesting a conserved role for IP6 in lentiviral assembly.},
  author       = {Dick, Robert A. and Xu, Chaoyi and Morado, Dustin R. and Kravchuk, Vladyslav and Ricana, Clifton L. and Lyddon, Terri D. and Broad, Arianna M. and Feathers, J. Ryan and Johnson, Marc C. and Vogt, Volker M. and Perilla, Juan R. and Briggs, John A. G. and Schur, Florian KM},
  issn         = {1553-7374},
  journal      = {PLOS Pathogens},
  number       = {1},
  publisher    = {Public Library of Science},
  title        = {{Structures of immature EIAV Gag lattices reveal a conserved role for IP6 in lentivirus assembly}},
  doi          = {10.1371/journal.ppat.1008277},
  volume       = {16},
  year         = {2020},
}