Malaria, one of the deadliest infectious diseases in the world, claims the life of
hundreds of thousands of people each year. In 2019 According to WHO, there were
229 million malaria cases and 409 thousand deaths reported around the world. The
deadliest malaria causing agent is Plasmodium falciparum, a protozoan parasite that
infects human red blood cells. The parasite’s violence is attributed to its ability to
suppress efficient response in the host, and therefore the host’s inability to fully
clear the parasites from the system. One of the main proteins involved in this
immune evasion is Plasmodium falciparum erythrocytes membrane protein 1
(PfEMP1) encoded by a multi-copy gene family named var. This family has a unique
regulation through mutually exclusive expression, that allows the parasite to present
only one variant at a time. Previous study in the lab found 3 potential proteins which
are in interaction with elements known to be related to the mutually exclusive
expression mechanism. Two of these proteins haven’t been characterized yet and
the third one, Ornithine Aminotransferase (OAT) has been characterized before but
its new role in mutually exclusive mechanism remains unclear. Preliminary results
showed a new cellular localization of OAT in early stages parasites, which may imply
on its novel role in the mutually exclusive mechanism. Also, we were able to
characterize the other 2 protein’s cellular localization and their expression profile
throughout the asexual life cycle of the parasite. Characterization of these proteins
will lead to better understanding of the parasite’s pathogenicity.