Characterization of adhesion ligand phosphorylation in the malaria parasite Plasmodium falciparum (Welch, 1897)

Beschreibung

Aims of this study: Phosphorylation is an essential protein modification and has a vital impact on the invasion process of the malaria parasite into the red blood cell. One kinease - PKA - was already proven to participate in invasion by phosphorylating the cytoplasmic domain of the essential invasion protein AMA1. This phosphorylation had tremendous impact on AMA1 function and substitution of the phosphoacceptor site leads to a loss of AMA1 function. This work analyzes phosphorylation of cytoplasmic domains of invasion related parasites ligands and the responsible kinases. It is focused on Rh2b.
Aims of this study: Phosphorylation is an essential protein modification and has a vital impact on the invasion process of the malaria parasite into the red blood cell. One kinease - PKA - was already proven to participate in invasion by phosphorylating the cytoplasmic domain of the essential invasion protein AMA1. This phosphorylation had tremendous impact on AMA1 function and substitution of the phosphoacceptor site leads to a loss of AMA1 function. This work analyzes phosphorylation of cytoplasmic domains of invasion related parasites ligands and the responsible kinases. It is focused on Rh2b.

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Klemens Engelberg

Themen in »Characterization of adhesion ligand phosphorylation in the malaria parasite Plasmodium falciparum (Welch, 1897)«

Malaria Plasmodium falciparum Rh2b cytoplasmic domain (CPD) phosphorylation reticulocyt binding homologue proteins (Rh)

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