Computational analysis of PhospholipaseA2 in the honey bee venom

Abstract

Honey bee venom (HBV) is composed of an intricate mixture of polypeptides, enzymes, amines, lipids, and amino acids. The principal enzyme present in HBV is Phospholipase A2 (PLA2). The present investigation includes retrieval of amino acid sequence information, sequence analysis and physicochemical characterization of PLA2 protein sequences of three honey bee species viz., Apis mellifera, Apis dorsata, and Apis cerana using computational tools retrieved from NCBI (National Centre for Biotechnology Information) protein sequence database. The physicochemical parameters viz., amino acid composition, molecular weight, isoelectric point, aliphatic index, hydropathicity were determined. The result of the primary structure analysis suggests that most of the PLA2 is hydrophobic due to the presence of high non-polar residues content. The isoelectric point predicted ranged from 7.05 to 8.65. The aliphatic index computed by Expasy’s Protparam infers that most of the PLA2 is stable at a wide range of temperatures (51.64–85.17). The secondary structure analysis by SOPMA showed that PLA2 contains more random-coils and alpha-helices than beta-sheets. SMART values revealed an expected range of 0.00000146–12. SVM prot analysis of proteins predicted that these proteins may act as drug targets for inflammatory response lipid-binding proteins, hydrolases, transferases and metal binding. Multiple Sequence alignment by MUSCLE tool revealed significantly conserved (Leucine) and semi-conserved regions (Proline, Alanine). Genebee service software was used to predict the RNA structure. The 3 D structure analysis of PLA2 was done by using SWISS-MODEL.

Keywords:

• honey bee venom
• phospholipase A2
• SVM prot
• ProtParam
• SMART
• SWISS-MODEL

Disclosure statement

No potential conflict of interest was reported by the authors.