Agricultural and Biological Sciences Journal
Articles Information
Agricultural and Biological Sciences Journal, Vol.5, No.2, Jun. 2019, Pub. Date: May 28, 2019
Prediction and Analysis of Key Sites for Hepatitis B Antigen-antibody Interactions: Computational Simulation
Pages: 50-59 Views: 118 Downloads: 104
[01] Linsong Yang, Biomedicine Laboratory, School of Pharmaceutical Engineering and Life Science, Changzhou University, Changzhou, China.
[02] Weiwei Ji, Biomedicine Laboratory, School of Pharmaceutical Engineering and Life Science, Changzhou University, Changzhou, China.
[03] Hui Zhong, Biomedicine Laboratory, School of Pharmaceutical Engineering and Life Science, Changzhou University, Changzhou, China.
[04] Fang Wang, Biomedicine Laboratory, School of Pharmaceutical Engineering and Life Science, Changzhou University, Changzhou, China.
The phenomenon of immune escape and diagnostic escape caused by mutations of "a" determinant region is becoming more and more frequent. It is now well established that the preS2 region has the highly immunogenicity. However, the mechanism of the preS2 as an antigen epitope interacting with antibody have been poorly investigated. The present study simulation analyzed the structure and immunogenic activity of the preS2 and predicted key sites for antigen-antibody interactions. Three-dimensional structure of the HBV envelope Large (preS1+preS2+S) protein was predicted and optimized using several web tools. Then we evaluated the quality of the 3D structure. After that we used protein-protein Docking module in BioLuminate software to analyze the docking of antigen antibodies and Residue Scanning in Maestro BioLuminate was used to replace some residues on the antigen by Alanine, respectively. Meanwhile, the CHARMm force field in DS software was used for molecular dynamics simulation analysis of composite surface interaction. MET120, GLN121, TRP122, ASN123, PHE127 and LEU132 on preS2 are key sites for interaction with antibodies. When these sites were replaced with alanine cause a considerable reduction in the tightness and stability of protein complexes. And these mutation in the preS2, leading to a reduced binging ability to its monoclonal antibody, F124. These data will be beneficial for designing more advanced antibodies. It has practical value in guiding experimenters to rationally design and analyze protein-protein interactions. The results of this study may assist in the design or development of more effective hepatitis B vaccines.
PreS2 Antigen, Residue Scanning, Computational Simulation, HBV Vaccines, Homology Modeling
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