Vol. 7, Issue 5 (2018)

Author(s):
Payal Kapoor, Arti Chauhan, Rachna Hora and Prakash Chandra Mishra

Abstract:
Alveolates (dinoflagellates, ciliates and apicomplexans) possess a characteristic cortical structure termed as the ‘pellicle’. Alveolate pellicle plays a structural role and helps define the cell shape in dinoflagellates and ciliates whereas in apicomplexans it plays an additional role in parasite motility and cytokinesis. The pellicle is composed of flattened membranous sacs which subtend immediately below the plasma membrane. These flattened sacs are termed as the ‘inner membrane complex’ (IMC) in apicomplexans. IMC proteins can be categorized according to their structural features into three groups namely multi-transmembrane proteins, alveolins and non-alveolins. Only a few members of IMC1 family of proteins are known in Plasmodium falciparum (Pf). Knock-out studies of IMC1 members in other Plasmodium species have demonstrated the role of these proteins in mechanical stability and motility of the parasite. Here, we used bioinformatics tools to gain insight into the structure of IMC1l. We predicted the partial 3 dimensional model of Pf IMC1l and propose that its α-helical region might be involved in binding to cytoskeletal proteins such as actin or myosin. The hydrophobic residues in the IMCp region of IMC1 proteins might be responsible for their attachment to the IMC membrane. PfIMC1 proteins were also found to have asparagine rich regions, N-or C-terminal palmitoylation sites and other motifs of functional significance. Being crucial structural elements of inner membrane complex, IMC1 proteins are likely to be potential antimalarial drug targets.