Volume 32, Issue 214 (11-2022)
J Mazandaran Univ Med Sci 2022, 32(214): 153-166 |
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Hasanshahi Z, Dehghani B, Hashempour T, Moayedi J. Bioinformatics Study of the Interaction between Melittin Protein and P24 Protein in HIV and SIV Viruses. J Mazandaran Univ Med Sci 2022; 32 (214) :153-166
URL: http://jmums.mazums.ac.ir/article-1-14040-en.html
URL: http://jmums.mazums.ac.ir/article-1-14040-en.html
Abstract: (791 Views)
Background and purpose: P24 is one of the important components of retroviruses capsid. Several studies have shown the inhibitory effect of melittin protein on the function of AIDS virus. The aim of this study was to evaluate the effect of this protein on P24 in SIV and HIV viruses using bioinformatics software.
Materials and methods: P24 protein sequences of SIV and HIV were obtained from a gene bank and their features were analyzed using different software programs. Also, structural similarities of P24 protein between SIV and HIV viruses were examined. Docking analysis was used to examine the interactions between melittin and P24 proteins. The stability of docking results were confirmed by molecular dynamics simulation.
Results: Findings showed numerous phosphorylation, glycosylation sites, and di-sulfide bonds in P24 protein. Docking results indicated a probable interaction between P24 protein of both viruses and melittin. The results showed similarity of the third structure of P24 protein between the two viruses. Analysis of molecular dynamics showed molecular stability of the interactions between P24 and melittin proteins.
Conclusion: High energy values of the interaction between melittin and P24 indicated high binding potential of the two proteins, which can determine the inhibitory effect of melittin on the function of HIV capsid. Analysis of the third structure of P24 protein in both viruses showed that they are very similar despite the high difference in protein sequences from the point of view of folding and 3D structure. Application of melittin to control SIV infections in primates can be used as a model for inhibiting HIV in humans.
Materials and methods: P24 protein sequences of SIV and HIV were obtained from a gene bank and their features were analyzed using different software programs. Also, structural similarities of P24 protein between SIV and HIV viruses were examined. Docking analysis was used to examine the interactions between melittin and P24 proteins. The stability of docking results were confirmed by molecular dynamics simulation.
Results: Findings showed numerous phosphorylation, glycosylation sites, and di-sulfide bonds in P24 protein. Docking results indicated a probable interaction between P24 protein of both viruses and melittin. The results showed similarity of the third structure of P24 protein between the two viruses. Analysis of molecular dynamics showed molecular stability of the interactions between P24 and melittin proteins.
Conclusion: High energy values of the interaction between melittin and P24 indicated high binding potential of the two proteins, which can determine the inhibitory effect of melittin on the function of HIV capsid. Analysis of the third structure of P24 protein in both viruses showed that they are very similar despite the high difference in protein sequences from the point of view of folding and 3D structure. Application of melittin to control SIV infections in primates can be used as a model for inhibiting HIV in humans.
Type of Study: Research(Original) |
Subject:
Medical Virology
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