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Characterization of Toxoplasma DegP, a rhoptry serine protease crucial for lethal infection in mice.

Abstract During the infection process, Apicomplexa discharge their secretory organelles called micronemes, rhoptries and dense granules to sustain host cell invasion, intracellular replication and to modulate host cell pathways and immune responses. Herein, we describe the Toxoplasma gondii Deg-like serine protein (TgDegP), a rhoptry protein homologous to High temperature requirement A (HtrA) or Deg-like family of serine proteases. TgDegP undergoes processing in both types I and II strains as most of the rhoptries proteins. We show that genetic disruption of the degP gene does not impact the parasite lytic cycle in vitro but affects virulence in mice. While in a type I strain DegPI appears dispensable for the establishment of an infection, removal of DegPII in a type II strain dramatically impairs the virulence. Finally, we show that KO-DegPII parasites kill immunodeficient mice as efficiently as the wild-type strain indicating that the protease might be involved in the complex crosstalk that the parasite engaged with the host immune response. Thus, this study unravels a novel rhoptry protein in T. gondii important for the establishment of lethal infection.
PMID
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Authors

Mayor MeshTerms
Keywords
Journal Title plos one
Publication Year Start




PMID- 29244879
OWN - NLM
STAT- MEDLINE
DCOM- 20180105
LR  - 20180105
IS  - 1932-6203 (Electronic)
IS  - 1932-6203 (Linking)
VI  - 12
IP  - 12
DP  - 2017
TI  - Characterization of Toxoplasma DegP, a rhoptry serine protease crucial for lethal
      infection in mice.
PG  - e0189556
LID - 10.1371/journal.pone.0189556 [doi]
AB  - During the infection process, Apicomplexa discharge their secretory organelles
      called micronemes, rhoptries and dense granules to sustain host cell invasion,
      intracellular replication and to modulate host cell pathways and immune
      responses. Herein, we describe the Toxoplasma gondii Deg-like serine protein
      (TgDegP), a rhoptry protein homologous to High temperature requirement A (HtrA)
      or Deg-like family of serine proteases. TgDegP undergoes processing in both types
      I and II strains as most of the rhoptries proteins. We show that genetic
      disruption of the degP gene does not impact the parasite lytic cycle in vitro but
      affects virulence in mice. While in a type I strain DegPI appears dispensable for
      the establishment of an infection, removal of DegPII in a type II strain
      dramatically impairs the virulence. Finally, we show that KO-DegPII parasites
      kill immunodeficient mice as efficiently as the wild-type strain indicating that 
      the protease might be involved in the complex crosstalk that the parasite engaged
      with the host immune response. Thus, this study unravels a novel rhoptry protein 
      in T. gondii important for the establishment of lethal infection.
FAU - Lentini, Gaelle
AU  - Lentini G
AUID- ORCID: http://orcid.org/0000-0003-0836-9972
AD  - UMR 5235 CNRS, Universite de Montpellier, Montpellier, France.
FAU - El Hajj, Hiba
AU  - El Hajj H
AD  - Department of Internal Medicine and Experimental Pathology, Immunology and
      Microbiology, American University of Beirut, Beirut, Lebanon.
FAU - Papoin, Julien
AU  - Papoin J
AD  - UMR 5235 CNRS, Universite de Montpellier, Montpellier, France.
FAU - Fall, Gamou
AU  - Fall G
AD  - UMR 5235 CNRS, Universite de Montpellier, Montpellier, France.
FAU - Pfaff, Alexander W
AU  - Pfaff AW
AD  - Institut de Parasitologie et Pathologie Tropicale, EA 7292, Federation de
      Medecine Translationnelle, Universite de Strasbourg, Strasbourg, France.
FAU - Tawil, Nadim
AU  - Tawil N
AD  - Department of Internal Medicine and Experimental Pathology, Immunology and
      Microbiology, American University of Beirut, Beirut, Lebanon.
FAU - Braun-Breton, Catherine
AU  - Braun-Breton C
AD  - UMR 5235 CNRS, Universite de Montpellier, Montpellier, France.
FAU - Lebrun, Maryse
AU  - Lebrun M
AUID- ORCID: http://orcid.org/0000-0002-0962-0156
AD  - UMR 5235 CNRS, Universite de Montpellier, Montpellier, France.
LA  - eng
PT  - Journal Article
DEP - 20171215
PL  - United States
TA  - PLoS One
JT  - PloS one
JID - 101285081
RN  - 0 (Protozoan Proteins)
RN  - EC 3.4.- (Serine Proteases)
SB  - IM
MH  - Animals
MH  - Mice, Inbred BALB C
MH  - Mice, Inbred NOD
MH  - Mice, SCID
MH  - Protein Processing, Post-Translational
MH  - Proteolysis
MH  - Protozoan Proteins/*physiology
MH  - Serine Proteases/*physiology
MH  - Toxoplasma/*enzymology/genetics/pathogenicity
MH  - Toxoplasmosis/*parasitology
MH  - Virulence
PMC - PMC5731766
EDAT- 2017/12/16 06:00
MHDA- 2018/01/06 06:00
CRDT- 2017/12/16 06:00
PHST- 2017/08/10 00:00 [received]
PHST- 2017/11/27 00:00 [accepted]
PHST- 2017/12/16 06:00 [entrez]
PHST- 2017/12/16 06:00 [pubmed]
PHST- 2018/01/06 06:00 [medline]
AID - 10.1371/journal.pone.0189556 [doi]
AID - PONE-D-17-29630 [pii]
PST - epublish
SO  - PLoS One. 2017 Dec 15;12(12):e0189556. doi: 10.1371/journal.pone.0189556.
      eCollection 2017.