جستجوی مقالات مرتبط با کلیدواژه "vp28" در نشریات گروه "دامپزشکی"

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.