Document Type : Full Research Paper
Authors
1
Department of Basic Sciences, Faculty of Veterinary Medicine, Lorestan University, Khorramabad, Iran.
2
Department of Basic Sciences, Faculty of Veterinary Medicine, Lorestan University, Khorramabad, Iran
3
Department of Microbiology and Food Health, Faculty of Veterinary Medicine, Lorestan University, Khorramabad, Iran.
Abstract
The White spot syndrome virus (WSSV) has emerged as one of the most prevalent, widespread and lethal pathogens in shrimp. The virus gains entry into the shrimps trough binding membrane protein VP28,thereby initiatingan infection. The present study started with a re-examination of the antimicrobial properties of each peptides by the Peptide Scanner server. This was followed by an evaluation of the physicochemical characteristics, solubility, allergenicity, and also the toxicity of the antiviral peptides by the ProtParam, Protein-Sol, AllerTOP,and ToxinPred servers respectively. Subsequently, the third structure of peptides identified in the preceding steps, comprising Ginkbilobin, Circulin-F, Cycloviolin-A, Cycloviolin-D, Circulin-C, Kalata-B8 and Antiviral protein Y3, was predicted by the I-TASSER server. The results of the molecular docking process of each peptide with VP28 protein showed that the mentioned peptides formed 4, 1, 2, 0, 1, 4 and 10 hydrogen bonds with VP28 protein, respectively. In addition, each of them contains 25.50, 41.38, 38.71, 36.67, 33.33, 16.13 and 36.08 percent hydrophobic amino acids, respectively. Ultimately, the Antiviral protein Y3 peptide is the most promising option, followed by Ginkbilobin and Kalata-B8 peptides, due to its length, the presence of hydrophobic amino acids, and the number of hydrogen bonds formed with the VP28 protein. Consequently, following the completion of the molecular dynamics studies, it is recommended that the aforementioned peptides be employed in in -vitro and in vivo investigations aimed at impeding the invasion of WSSV into the shrimp host and subsequently preventing infection.
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