Abstract
Computational protein sequence analysis is one of the most important tools used for understanding the evolution of closely related proteins sequences including snake venom metalloproteinase sequences (SVMPs) which give valuable information regarding genetic variations. The fundamental objective of the present study is to screen the evolution distributed in metalloproteinase domain regions of protein sequences among different SVMPs in snake species which are involved in a range of pathological disorders such as arthritis, atherosclerosis, liver fibrosis, cardiovascular, cancer, liver and neurodegenerative disorders. In fact, SVMPS are responsible for hemorrhage and may also interfere with the hemostatic system. A comparative characterization of the metalloproteinase sequences has been carried out to analyze their multiple sequence alignment, phylogenic tree, homology, physicochemical, secondary structural and functional properties. DNAMAN software was used for multiple sequence alignment, phylogenic tree and homology and Expasy’s Prot-param server was used for amino acid composition, physico-chemical and functional characterization of these SVMPs sequences. Studies of secondary structure of these SVMPs were carried out by computational program. Based on the observed patterns of occurrence of atypical features, we hypothesize that amino acids of metalloproteinase domain region (66.63% identity) of protein sequences are highly changeable; whereas, signal peptide region (93.98% identity) is the lowest changeable protein sequence and the remaining other three domains such as propeptide region (87.36% identity), desintegrin domain region (78.63% identity) and cysteine-rich domain region (75.70% identity) show moderate changeable protein sequence. SVMPs might be an accelerated evolution, which is a key player in causing diseases. From the data, it can be suggested that over -changed metalloproteinase domain regions in snake venom metalloproteinase might be responsible for the generation of functional variation of proteins expressed, which in turn may lead to different disorders in humans after snake bite. The results of this study would be an effective tool for the study of mutation, drugs resistance mechanisms and development of new drugs for different diseases. Key words : SVMPs, evolution, multiple sequence alignment, phylogenic tree, secondary structure, homology.
Highlights
Metalloproteinase is a ubiquitous enzyme that exists in most organisms from animal to plants
The fundamental objective of the present study is to screen the evolution distributed in metalloproteinase domain regions of protein sequences among different Snake venom metalloproteinase sequences (SVMP) in snake species which are involved in a range of pathological disorders such as arthritis, atherosclerosis, liver fibrosis, cardiovascular, cancer, liver and neurodegenerative disorders
The National Center for Biotechnology Information (NCBI) database was used as source to collect SVMPs sequences from different venomous snake species with accession number (Table 1)
Summary
Metalloproteinase is a ubiquitous enzyme that exists in most organisms from animal to plants. Apart from its different expression sites in different plants and animals for performing distinct physiological roles, metalloproteinase exists in the toxin/venom of several venomous creatures (snake, caterpillar, scorpion etc.) to cause agony, suffering and even death of the prey/victim. Several diseases are shown to be associated with metalloproteinase. Genetic polymorphisms in matrix metalloproteinase genes MMP1, MMP9 and MMP12 are shown to be important in the development of chronic obstructive pulmonary disease (COPD) (Wallace and Sandford, 2002). Metalloproteinases play role in the development of renal cyst (Obermüller et al, 2001), uterine cervical carcinoma (Libra et al, 2009), angiogenesis (Pepper, 2001) and various inflammatory diseases of the central nervous system such as bacterial meningitis
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