Molecular Chaperones and Parasites

Molecular Chaperones and Parasites

Molecular chaperones and chaperonins are proteins found in all living organisms from the prokaryotic bacteria all the way to the eukaryotic human. These proteins serve to play several important roles within the cell. The tasks vary from assisting directly or indirectly in the folding of nascent proteins produced by the ribosome, repairing heat damaged proteins, involvement in cell signaling, and cell differentiation. Many of these proteins are inducible in response to heat. Therefore they became known as heat shock proteins (Hsp). Proteins are absolutely vital in any cell. They serve specific structural and functional roles to enable cellular life. Currently, scientists know basically how chaperones and chaperonins work, but the complete mechanism is still unknown. ATP hydrolysis is seen to be implicated in changing the conformation of chaperonins which therefore alter the conformation of the nascent protein. Chaperones and Chaperonins are currently being implicated in studies to further understand their roles in some common human parasitic organisms. The primary three parasites investigated in this review of the literature are Plasmodium falciparum (P. falciparum), Trypanosoma cruzi (T. cruzi), and Leishmania donovani (L. donovani). Each parasite is known to cause malaria, Chagas disease (African sleeping sickness), and Leishmaniasis respectively. Another parasite,Entanoeba histolytica is briefly discussed as well. This literature review will further examine the various Hsps in these parasites and outline their function as well as implications for medical treatment and further research.