نوع مقاله : مقاله پژوهشی
نویسندگان
1 دانشجوی دکتری ، گروه علوم دامی، دانشکده کشاورزی، دانشگاه فردوسی مشهد
2 استاد، گروه علوم دامی، دانشکده کشاورزی، دانشگاه فردوسی مشهد
چکیده
کلیدواژهها
عنوان مقاله [English]
نویسندگان [English]
Background and objectives: Bovine diarrhea is a common disease among calves that causes significant economic losses in the dairy and meat industry because of increased mortality, treatment costs and reduced growth rates and increasing age at first calving. Bovine rotavirus is one of the main causes of diarrhea in calves at the age of one to two weeks. Both vp4 and vp7 proteins form the outer capsid of the virus, producing antibodies and stimulating the immune system. Camel lactoferrampine-Lactoferrin is a potent antiviral that binds to heparin proteoglycine sulfate, prevents virus entry into the host cell and can replace antiviral drugs. The aim of this study was to investigate the possibility of replacement of camel lactoferrin peptide with antiviral drugs.
Materials and methods: In this study, the possibility of replacing six recombinant camel lactoferrin peptides named clf36-1, clf36-2, 12A-36F + BC, A_Scaning, AF, Arm with antiviral drugs and efficient binding of these peptides to Surface proteins of bovine rotavirus (vp4 and vp7) was investigated by molecular dynamics simulation using GROMACS software and they were compared due to their bond-dissociation energy in docking step and amount of electric charge before Neutralizing the electric charge of systems in molecular dynamics and finally the best substituted peptide was selected according to Radius of gyration diagram which is the main determinative factor in system efficiency in vivo and also indicates the possibility of stable binding of recombinant lactoferrin peptide to the virus’ surface protein.
Results: The results of this study indicate that the lactoferrin peptide binds well with the rotavirus’ surface proteins and can thus prevent the virus from entering the cells. However, among the six peptides examined, the 12A-36F + BC peptide in both vp4 and vp7 systems seems to be inefficient in vivo in spite of the highest bond-dissociation energy and the most positive electric charge before Neutralizing the electric charge of systems in molecular dynamics. As being unfold and Rg fluctuation during the simulation. Hence this study expects that recombinant peptide clf36-1 and vp4 system will bind well according to the Radius of gyration diagram.
Conclusions: The results of this study show that the clf36-1 peptide was stable and efficiently bound to vp4 surface protein among the six peptides investigated while retaining its structure during the simulation and in this way it can prevent the virus from entering the cells. So it can be an appropriate alternative to antiviral drugs. However, in vivo experiments are needed to prove the efficacy of this peptide.
کلیدواژهها [English]
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