Successful modification | The parasite was generated by the genetic modification |
The mutant contains the following genetic modification(s) |
Gene tagging,
Introduction of a transgene
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Reference (PubMed-PMID number) |
Not published (yet)
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MR4 number |
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Parent parasite used to introduce the genetic modification |
Rodent Malaria Parasite | P. berghei |
Parent strain/line | P. berghei ANKA |
Name parent line/clone |
Not applicable
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Other information parent line | |
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The mutant parasite was generated by |
Name PI/Researcher | Laine C, Khalife J, Pierrot C |
Name Group/Department | CIIL - Center for Infection and Immunity of Lille |
Name Institute | Univ. Lille, CNRS, Inserm, CHU Lille, Institute Pasteur de Lille |
City | Lille |
Country | France |
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Name of the mutant parasite |
RMgm number | RMgm-5369 |
Principal name | PbRpt3-mCherry |
Alternative name | |
Standardized name | |
Is the mutant parasite cloned after genetic modification | Yes |
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Phenotype |
Asexual blood stage | PbRpt3 localization was then assessed by immunofluorescence assays. Low expression in early trophozoite stages which strongly increases during the late trophozoite stages. In schizonts, the signal corresponding to PbRpt3-mCherry seems to be less intense. Concerning the cellular distribution of PbRpt3-mCherry, it is mainly cytoplasmic in trophozoites and schizonts stages, with a punctuated localization particularly in late trophozoites. |
Gametocyte/Gamete | Gametocytes show a high level of PbRpt3-mCherry expression. In gametocytes, the IFA signal overlaps with DAPI staining, indicating that PbRpt3 is more accumulated in the nucleus at this stage |
Fertilization and ookinete | Not tested |
Oocyst | Not tested |
Sporozoite | Not tested |
Liver stage | Not tested |
Additional remarks phenotype | Mutant/mutation
The mutant expresses a C-terminal mCherry-tagged version of PbRpt3 and expresses GFP under the constitutive hsp70 promoter
Protein (function)
The 26S proteasome is the main proteolytic machine involved in protein degradation. This macromolecular complex, consisting of a 20S core parcle assembled with one or two 19S regulatory particles, is highly regulated by phosphorylation. In the paper evidence is presented that i) the P. berghei proteasome AAA-ATPase regulatory subunit Rpt3 is highly regulated by phosphorylation; ii) that it binds to protein phosphatase 1, the major parasite phosphatase and iii) that PbRpt3 regulates the activity of the phosphatase both in vitro and in a heterologous model of Xenopus oocytes
Phenotype
PbRpt3 localization was then assessed by immunofluorescence assays. Low expression in early trophozoite stages which strongly increases during the late trophozoite stages. In schizonts, the signal corresponding to PbRpt3-mCherry seems to be less intense. Concerning the cellular distribution of PbRpt3-mCherry, it is mainly cytoplasmic in trophozoites and schizonts stages, with a punctuated localization particularly in late trophozoites.
Gametocytes show a high level of PbRpt3-mCherry expression. In gametocytes, the IFA signal overlaps with DAPI staining, indicating that PbRpt3 is more accumulated in the nucleus at this stage.
Additional information
Other mutants |