---
_id: '15276'
abstract:
- lang: eng
text: 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 Ustilago maydis,
effector-coding genes frequently organize in clusters. Here we describe the functional
characterization of the pleiades, a cluster of ten
effector genes, by analyzing the micro- and macroscopic phenotype of the cluster
deletion and expressing these proteins in planta. Deletion
of the pleiades 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.
article_number: e1009641
article_processing_charge: Yes
article_type: original
author:
- first_name: Fernando
full_name: Navarrete, Fernando
last_name: Navarrete
- first_name: Nenad
full_name: Grujic, Nenad
last_name: Grujic
- first_name: Alexandra
full_name: Stirnberg, Alexandra
last_name: Stirnberg
- first_name: Indira
full_name: Saado, Indira
last_name: Saado
- first_name: David
full_name: Aleksza, David
last_name: Aleksza
- first_name: Michelle C
full_name: Gallei, Michelle C
id: 35A03822-F248-11E8-B48F-1D18A9856A87
last_name: Gallei
orcid: 0000-0003-1286-7368
- first_name: Hazem
full_name: Adi, Hazem
last_name: Adi
- first_name: André
full_name: Alcântara, André
last_name: Alcântara
- first_name: Mamoona
full_name: Khan, Mamoona
last_name: Khan
- first_name: Janos
full_name: Bindics, Janos
last_name: Bindics
- first_name: Marco
full_name: Trujillo, Marco
last_name: Trujillo
- first_name: Armin
full_name: Djamei, Armin
last_name: Djamei
citation:
ama: Navarrete F, Grujic N, Stirnberg A, et al. The Pleiades are a cluster of fungal
effectors that inhibit host defenses. PLOS Pathogens. 2021;17(6). doi:10.1371/journal.ppat.1009641
apa: Navarrete, F., Grujic, N., Stirnberg, A., Saado, I., Aleksza, D., Gallei, M.
C., … Djamei, A. (2021). The Pleiades are a cluster of fungal effectors that inhibit
host defenses. PLOS Pathogens. Public Library of Science. https://doi.org/10.1371/journal.ppat.1009641
chicago: Navarrete, Fernando, Nenad Grujic, Alexandra Stirnberg, Indira Saado, David
Aleksza, Michelle C Gallei, Hazem Adi, et al. “The Pleiades Are a Cluster of Fungal
Effectors That Inhibit Host Defenses.” PLOS Pathogens. Public Library of
Science, 2021. https://doi.org/10.1371/journal.ppat.1009641.
ieee: F. Navarrete et al., “The Pleiades are a cluster of fungal effectors
that inhibit host defenses,” PLOS Pathogens, vol. 17, no. 6. Public Library
of Science, 2021.
ista: Navarrete F, Grujic N, Stirnberg A, Saado I, Aleksza D, Gallei MC, Adi H,
Alcântara A, Khan M, Bindics J, Trujillo M, Djamei A. 2021. The Pleiades are a
cluster of fungal effectors that inhibit host defenses. PLOS Pathogens. 17(6),
e1009641.
mla: Navarrete, Fernando, et al. “The Pleiades Are a Cluster of Fungal Effectors
That Inhibit Host Defenses.” PLOS Pathogens, vol. 17, no. 6, e1009641,
Public Library of Science, 2021, doi:10.1371/journal.ppat.1009641.
short: F. Navarrete, N. Grujic, A. Stirnberg, I. Saado, D. Aleksza, M.C. Gallei,
H. Adi, A. Alcântara, M. Khan, J. Bindics, M. Trujillo, A. Djamei, PLOS Pathogens
17 (2021).
date_created: 2024-04-03T08:00:34Z
date_published: 2021-06-24T00:00:00Z
date_updated: 2024-04-09T10:26:12Z
day: '24'
ddc:
- '580'
department:
- _id: JiFr
doi: 10.1371/journal.ppat.1009641
external_id:
pmid:
- '34166468'
file:
- access_level: open_access
checksum: ab8428291a0c14607c4ea5656c029cff
content_type: application/pdf
creator: dernst
date_created: 2024-04-09T10:24:43Z
date_updated: 2024-04-09T10:24:43Z
file_id: '15305'
file_name: 2021_PlosPathogens_Navarrete.pdf
file_size: 2616563
relation: main_file
success: 1
file_date_updated: 2024-04-09T10:24:43Z
has_accepted_license: '1'
intvolume: ' 17'
issue: '6'
keyword:
- Virology
- Genetics
- Molecular Biology
- Immunology
- Microbiology
- Parasitology
language:
- iso: eng
month: '06'
oa: 1
oa_version: Published Version
pmid: 1
publication: PLOS Pathogens
publication_identifier:
issn:
- 1553-7374
publication_status: published
publisher: Public Library of Science
quality_controlled: '1'
status: public
title: The Pleiades are a cluster of fungal effectors that inhibit host defenses
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 17
year: '2021'
...
---
_id: '7464'
abstract:
- lang: eng
text: '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.'
acknowledged_ssus:
- _id: ScienComp
article_number: e1008277
article_processing_charge: No
article_type: original
author:
- first_name: Robert A.
full_name: Dick, Robert A.
last_name: Dick
- first_name: Chaoyi
full_name: Xu, Chaoyi
last_name: Xu
- first_name: Dustin R.
full_name: Morado, Dustin R.
last_name: Morado
- first_name: Vladyslav
full_name: Kravchuk, Vladyslav
id: 4D62F2A6-F248-11E8-B48F-1D18A9856A87
last_name: Kravchuk
orcid: 0000-0001-9523-9089
- first_name: Clifton L.
full_name: Ricana, Clifton L.
last_name: Ricana
- first_name: Terri D.
full_name: Lyddon, Terri D.
last_name: Lyddon
- first_name: Arianna M.
full_name: Broad, Arianna M.
last_name: Broad
- first_name: J. Ryan
full_name: Feathers, J. Ryan
last_name: Feathers
- first_name: Marc C.
full_name: Johnson, Marc C.
last_name: Johnson
- first_name: Volker M.
full_name: Vogt, Volker M.
last_name: Vogt
- first_name: Juan R.
full_name: Perilla, Juan R.
last_name: Perilla
- first_name: John A. G.
full_name: Briggs, John A. G.
last_name: Briggs
- first_name: Florian KM
full_name: Schur, Florian KM
id: 48AD8942-F248-11E8-B48F-1D18A9856A87
last_name: Schur
orcid: 0000-0003-4790-8078
citation:
ama: Dick RA, Xu C, Morado DR, et al. Structures of immature EIAV Gag lattices reveal
a conserved role for IP6 in lentivirus assembly. PLOS Pathogens. 2020;16(1).
doi:10.1371/journal.ppat.1008277
apa: Dick, R. A., Xu, C., Morado, D. R., Kravchuk, V., Ricana, C. L., Lyddon, T.
D., … Schur, F. K. (2020). Structures of immature EIAV Gag lattices reveal a conserved
role for IP6 in lentivirus assembly. PLOS Pathogens. Public Library of
Science. https://doi.org/10.1371/journal.ppat.1008277
chicago: Dick, Robert A., Chaoyi Xu, Dustin R. Morado, Vladyslav Kravchuk, Clifton
L. Ricana, Terri D. Lyddon, Arianna M. Broad, et al. “Structures of Immature EIAV
Gag Lattices Reveal a Conserved Role for IP6 in Lentivirus Assembly.” PLOS
Pathogens. Public Library of Science, 2020. https://doi.org/10.1371/journal.ppat.1008277.
ieee: R. A. Dick et al., “Structures of immature EIAV Gag lattices reveal
a conserved role for IP6 in lentivirus assembly,” PLOS Pathogens, vol.
16, no. 1. Public Library of Science, 2020.
ista: Dick RA, Xu C, Morado DR, Kravchuk V, Ricana CL, Lyddon TD, Broad AM, Feathers
JR, Johnson MC, Vogt VM, Perilla JR, Briggs JAG, Schur FK. 2020. Structures of
immature EIAV Gag lattices reveal a conserved role for IP6 in lentivirus assembly.
PLOS Pathogens. 16(1), e1008277.
mla: Dick, Robert A., et al. “Structures of Immature EIAV Gag Lattices Reveal a
Conserved Role for IP6 in Lentivirus Assembly.” PLOS Pathogens, vol. 16,
no. 1, e1008277, Public Library of Science, 2020, doi:10.1371/journal.ppat.1008277.
short: R.A. Dick, C. Xu, D.R. Morado, V. Kravchuk, C.L. Ricana, T.D. Lyddon, A.M.
Broad, J.R. Feathers, M.C. Johnson, V.M. Vogt, J.R. Perilla, J.A.G. Briggs, F.K.
Schur, PLOS Pathogens 16 (2020).
corr_author: '1'
date_created: 2020-02-06T18:47:17Z
date_published: 2020-01-27T00:00:00Z
date_updated: 2025-04-15T08:24:51Z
day: '27'
ddc:
- '570'
department:
- _id: FlSc
doi: 10.1371/journal.ppat.1008277
external_id:
isi:
- '000510746400010'
pmid:
- '31986188'
file:
- access_level: open_access
checksum: a297f54d1fef0efe4789ca00f37f241e
content_type: application/pdf
creator: dernst
date_created: 2020-02-11T10:07:28Z
date_updated: 2020-07-14T12:47:59Z
file_id: '7484'
file_name: 2020_PLOSPatho_Dick.pdf
file_size: 4551246
relation: main_file
file_date_updated: 2020-07-14T12:47:59Z
has_accepted_license: '1'
intvolume: ' 16'
isi: 1
issue: '1'
language:
- iso: eng
month: '01'
oa: 1
oa_version: Published Version
pmid: 1
project:
- _id: 26736D6A-B435-11E9-9278-68D0E5697425
call_identifier: FWF
grant_number: P31445
name: Structural conservation and diversity in retroviral capsid
publication: PLOS Pathogens
publication_identifier:
issn:
- 1553-7374
publication_status: published
publisher: Public Library of Science
quality_controlled: '1'
related_material:
record:
- id: '9723'
relation: research_data
status: deleted
scopus_import: '1'
status: public
title: Structures of immature EIAV Gag lattices reveal a conserved role for IP6 in
lentivirus assembly
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 16
year: '2020'
...