<i>In-silico</i> Characterization and 3D Structure Prediction of MX Protein of<i> Lates Calcarifer (Barramundi)</i>: A Major Threat to Aqua Industry

Authors

DOI:

https://doi.org/10.18311/ti/2018/v25i4/24029

Keywords:

Barramundi, Betanoda Virus, Ligand, MX Protein, Viral Nervous Necrosis

Abstract

Betanoda virus is one of the most important and emerging groups of viruses known to infect around 40 species found to be worldwide in distribution. The most common and virulent target of infection for this virus is (Lates Calcarifer) (barramundi). It is found that the expression of MX protein is found to be the more susceptible reason for this viral infection. Considering this current study including characterization to structure prediction revolves around the MX protein as a target. The progression of this study describes the amino acid sequence of MX protein was retrieved from UniProt database in Fasta format and further primary structure analysis and characterization including nature of amino acids, instability index reading, GRAVY, determination of phosphorylation as well as signal peptide cleavage sites was done with the help of various tools. Secondary structure prediction has proceeded through SOPMA server analysis revealed that MX protein has mixed secondary structure, i.e., mostly alpha-helix and beta-turn. The progression of this work prediction of a 3D structure along with functional site prediction of MX protein of Fish (Lates Calcarifer) is done through standard modeling tools. The 3D structure of this protein of (Lates Calcarifer) as documented in this study may provide a valuable aid for designing an inhibitor or better ligand against viral nervous necrosis disease and could play a vital role in drug design.

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Published

2019-10-22

How to Cite

Singh, R., Prasad, K. P., Pathak, A., & Srivastava, P. (2019). <i>In-silico</i> Characterization and 3D Structure Prediction of MX Protein of<i> Lates Calcarifer (Barramundi)</i>: A Major Threat to Aqua Industry. Toxicology International, 25(4), 232–239. https://doi.org/10.18311/ti/2018/v25i4/24029