DOI: 10.5176/2251-2489_BioTech15.13
Authors: Roneet Choudhary, Arvind Agrawal, Shreya A Varghese and Mrs. Priya Swaminathan
Abstract: This study involves identifying antigenic regions of dihyroorotate dehydrogenase (DHODH) enzyme of parasitic organisms mainly Plasmodium falciparum and Plasmodium vivax. DHODH is an enzyme that catalyzes the fourth step of the de novo synthesis of pyrimidine. It is a flavo protein which is a commonly used target for drug designing in Malaria. The DHODH sequences of the above mentioned organisms were taken from NCBI and subjected for a multiple sequence alignment to determine shared conserved regions between Humans and Plasmodium. The sequences of organisms Plasmodium falciparum and Plasmodium vivax where then subjected to online MHC I and MHC II binding region predictor tools, PROPRED and PROPRED 1. The peptides which were most promiscuous (identified by multiple MHC I and MHC II alleles) and common for the two organisms were considered. The sequences were also subjected to other online tools like TAPPRED and NETCHOP, which predict the specificity of transport associated proteins and proteasome cleavage respectively. The shared peptides from PROPRED, PROPRED 1, TAPPRED and NETCHOP were shortlisted, for the given organisms. The final step was to determine whether the promiscuous peptides do not align with conserved Human sequences. Thus only one peptide was found to be most antigenic, promiscuous and common for the two Plasmodium’s which could be good vaccine candidates for Malaria.
Keywords: DHODH, Plasmodium, Malaria, Peptide, Vaccine
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