| Successful modification | The parasite was generated by the genetic modification |
| The mutant contains the following genetic modification(s) |
Gene disruption
|
| Reference (PubMed-PMID number) |
Reference 1 (PMID number) : 27387533
|
| MR4 number |
|
| top of page |
| Parent parasite used to introduce the genetic modification |
| Rodent Malaria Parasite | P. yoelii |
| Parent strain/line | P. y. yoelii 17XNL |
| Name parent line/clone |
Not applicable
|
| Other information parent line | |
| top of page |
| The mutant parasite was generated by |
| Name PI/Researcher | Hart RJ; Aly AS |
| Name Group/Department | Department of Tropical Medicine |
| Name Institute | Tulane University |
| City | New Orleans |
| Country | USA |
| top of page |
| Name of the mutant parasite |
| RMgm number | RMgm-1496 |
| Principal name | Pyadometdc/odc(–) |
| Alternative name | |
| Standardized name | |
| Is the mutant parasite cloned after genetic modification | Yes |
| top of page |
| Phenotype |
| Asexual blood stage | Reduced growth/asexual multiplication in mice. (Light-microscopic) morphology of blood stages was not different from wild type. |
| Gametocyte/Gamete | Reduced gametocyte production. Reduction in male gametocytes higher than in female gametocytes. Reduced male gamete formation (male gametogenesis/exflagellation). |
| Fertilization and ookinete | No ookinete formation in A. stephensi mosquitoes |
| Oocyst | No oocyst formation in A. stephensi mosquitoes |
| Sporozoite | No sporozoite formation in A. stephensi mosquitoes |
| Liver stage | Not tested |
| Additional remarks phenotype | Mutant/mutation
The mutant lacks expression of AdoMetDC/ODC
Protein (function)
Polyamines are positively-charged organic molecules that are important for cellular growth and division. Polyamines and their synthesizing enzymes are particularly abundant in rapidly proliferating eukaryotic cells such as parasitic protozoa and cancer cells. The three polyamine molecules (the diamine putrescine, the triamine spermidine and the tetramine spermine) are aliphatic positively charged molecules. No specific molecular physiological roles have yet been assigned to polyamines. Plasmodium is the only known living organism that has one open reading frame encoding two enzymes of this pathway, which are S-adenosyl methionine decarboxylase (AdoMetDC) and ODC. Both decarboxylase domains on the same protein were shown to be functionally and biochemically independent from each other. AdoMetDC converts adenosyl methionine into decarboxylated adenosyl methionine (dcAdoMet) and ODC converts ornithine into the diamine putrescine. Both putrescine and dcAdoMet are obligate substrates for the de novo biosynthesis of spermidine by the enzyme spermidine synthase (SpdS). In Plasmodium, SpdS is suggested to be the main enzyme responsible for the biosynthesis of spermine, as the genomes of all species of the malaria parasite lack spermine synthase (SpmS) coding sequence In addition to the biosynthesis of polyamines, Plasmodium parasites are able to actively salvage polyamines from their hosts, through an unknown transporter.
Phenotype
Reduced growth/asexual multiplication in mice. (Light-microscopic) morphology of blood stages was not different from wild type. The ability to knockout PyAdoMetDC/ODC demonstrates that the de novo biosynthesis of the polyamine putrescine and dcAdoMet (the other substrate for spermidine biosynthesis) is not essential for survival of asexual blood stage parasites of P. yoelii.
Reduced gametocyte production. Reduction in male gametocytes higher than in female gametocytes. Reduced male gamete formation (male gametogenesis/exflagellation).
No ookinete, oocyst and sporozoite formation in A. stephensi mosquitoes.
Additional information
Other mutants |
*RMgm-1496
