Protein kinase 9 is not required for completion of the Plasmodium berghei life cycle

Microbiol Res. 2022 Jul;260:127051. doi: 10.1016/j.micres.2022.127051. Epub 2022 Apr 26.


Protein kinases uniquely expressed in Plasmodium represent attractive drug targets. Previous studies have reported that Plasmodium falciparum Protein kinase 9 (Pk9) phosphorylates regulatory serine 106 of the ubiquitin-conjugating enzyme (Ubc13) thereby negatively regulating its activity. We investigated the effect of Pk9 depletion and Ubc13 mutation at S106 on the progression of rodent malaria model P. berghei life cycle. Our studies demonstrate that while phosphorylation of the regulatory serine 106 of Ubc13 is essential in blood stages, the lack of Pk9 expression neither altered Ubc13 phosphorylation nor parasite viability at all life cycle stages, though Ubc13 and Pk9 showed co-localization in the cytosol of erythrocytic and liver stages. Further, phosphorylation of Ubc13 in the absence of Pk9 reiterated the redundancy of its regulation in P. berghei. These results highlight the indispensable role of Ubc13 in P. berghei life cycle and redundancy in its phosphorylation by protein kinase and reiterate the need to validate novel gene function through genetic approaches for drug development strategies.

Keywords: Phosphorylation; Plasmodium; Protein kinase 9; Sporozoites; Ubc13.

MeSH terms

  • Animals
  • Life Cycle Stages
  • Plasmodium berghei* / genetics
  • Plasmodium falciparum / genetics
  • Plasmodium falciparum / metabolism
  • Protein Kinases* / metabolism
  • Protozoan Proteins / genetics
  • Protozoan Proteins / metabolism
  • Serine


  • Protozoan Proteins
  • Serine
  • Protein Kinases