Functional analysis of the "Apical Membrane Antigen 1": Investigating the role of phosphorylation of the blood-stage vaccine candidate in the malaria parasite Plasmodium falciparum

• Applicant: Professor Dr. Tim-Wolf Gilberger
• Subject Area: Parasitology and Biology of Tropical Infectious Disease Pathogens
• Term: from 2010 to 2014
• Project identifier: Deutsche Forschungsgemeinschaft (DFG) - Project number 161304732

• Final Report Year: 2014

Final Report Abstract

Our comparative studies using two invasion related type 1 transmembrane proteins showed that both proteins are getting phosphorylated in the cytoplasmic domain. While at least two sequential phosphorylations of AMA-1 (S610 and T613) are a prerequisite for efficient invasion of the malaria parasite, the phosphorylation of Rh2b appears not to be linked to its function in this process. The separation of essential from apparently redundant phosphorylation sites in combination with the identification of the responsible kinases are instrumental in exploring individual enzymes like PKA as drug targets.

Publications

• (2013): Specific phosphorylation of the PfRh2b invasion ligand of Plasmodium falciparum. Biochem J. 452: 457- 66
  Engelberg K, Paul AS, Prinz B, Kono M, Ching W, Heincke D, Dobner T, Spielmann T, Duraisingh MT and Gilberger TW
  
• (2012): Timelapse imaging of red blood cell invasion by rodent malaria parasite. PlosOne 7: e50780
  Yahata, K, Treeck, M, Culleton, R, Gilberger, TW and Kaneko, O