Journal of Biotechnology & Biomaterials
Open Access

Abstract

Mosquitoes are vectors of many deadliest diseases-malaria, dengue, chicken guinea, Japanese encephalitis, yellow fever, etc. The endogenous peptides, which are constitutively expressed or induced, provide a fast and effective means of defense against the parasites to the mosquito. The use of bioinformatics tools for phylogenetic relationships of three antimicrobial peptides of mosquito, cecropin, defensin and gambicin based on amino acid sequence information was elucidated. The presence of non-polar residues in the primary structure of peptides confirm their hydrophobic nature. Conserved signature sequence motif, W-x(0,2)-[KDN]-{Q}-{L}-K-[KRE]-[LI]-E-[RKN] in N-terminal of cecropin and C-x(3)-C-x(6,9)-[GAS]-KC-[ IMQT]-x(3)-C-x-C in defensin is identified which is responsible for their antimicrobial nature. Mosquito defensin shows presence of cystein residues that may form disulphide bond and provide stability to antimicrobial peptide. The presence of catalytic and non-catalytic domains is in accordance with presence of conserved signature sequence. Gambicin is the novel antimicrobial as it does not show sequence similarity with any other antimicrobial gene. The study will leads to identification of novel antimicrobial compound which could be used as a drug in human against many pathogenic diseases.

Biography

Email: neelamsehrawat@gmail.com