HIV Capsid and Protease, New Targets of Melittin

Melittin is a 26 amino acid amphipathic peptide, the main part of a bee venom. It has been confirmed that melittin can act against a vast verity of infectious agents, such as human immunodeficiency virus (HIV). This study aimed to investigate all physicochemical properties, post-modification sites, and interactions between melittin and HIV proteins. Ten Melittin sequences from different honey bees were collected from NCBI genebank. The physicochemical properties were evaluated for all sequences, and phosphorylation sites, glycolization positions and disulfide bonds were determined. Signal peptide was predicted by SignalP, secondary and tertiary structures were constructed by different software. Docking and interaction analysis were done by HEX and Discovery Studio. Results showed that most mutations occurred inApis florae; this genotype was placed in a district clade in the cladogram. Physicochemical features showed melittin to be a basic protein and stable in prokaryotic and eukaryotic cells. It is an allergen peptide and no disulfide bonds and glycosylation site was found in its structure. Just one phosphorylation position was found and the majority of secondary structures are Alpha helix and Beta turn. High energy values of interactions belonged to capsid and protease proteins, and docking showed several amino acids to be involved in the interactions. Our observations suggested that in addition to envelope and long terminal repeat, capsid and proteases of HIV could have a great potential as a target for melittin. Our data provides a comprehensive understanding of melittin properties, structures, and its interaction with HIV proteins.