PfBDP1: A master regulator of red blood cell invasion genes

According to the World Health Organization’s estimates for 2021, cardiovascular disease ranks as the leading cause of death, responsible for more than 17.9 million global fatalities in 2019. The escalating incidence of cardiovascular diseases is concerning. Diet, lifestyle, and genetics are well known to predispose people to cardiovascular disease, but another major risk factor is exposure to infectious diseases. Plasmodium falciparum is a unicellular protozoan parasite that is the causal agent of malaria, which contributes to increased cardiac problems, especially in low- and middle-income countries. Infections by P. falciparum cause nearly half a billion malaria cases annually, which can have fatal consequences due its impact on multiple system functions, particularly in cardiac, renal, neurological, and respiratory organs. Plasmodium falciparum orchestrates its life cycle between humans and the anopheles mosquito. The symptoms of malaria are associated with repeated rounds of parasite replication, egress, and invasion into the human red blood cells (RBCs). At this stage, it consumes hemoglobin from RBCs, preventing it from providing oxygen to the heart and resulting in anemic heart failure. Furthermore, parasitized RBCs adhere to the walls of blood arteries in the heart and brain to avoid detection by the immune system, frequently causing inflammation and blood vessel obstruction in these essential organs. These infection-related problems are directly connected to parasite invasion of RBCs; consequently, understanding the critical elements involved in this process is necessary for developing therapeutic preventions. P. falciparum Bromodomain Protein 1 (PfBDP1) is a multi-domain nuclear protein with a unique sequence of seven ankyrin repeats followed by a bromodomain. PfBDP1 has been demonstrated in vivo to perform a direct role in parasite invasion of RBCs by modulating the expression of invasion-related genes. The conserved bromodomain region of PfBDP1 detects acetylated lysine modifications on histone proteins in the nucleosome. However, the molecular processes that drive ligand binding, and consequently regulate PfBDP1 activity, are yet unclear.

Basic Science

Jan 2024 — Dec 2025

$151,564

United States