Abstract
Background: The mutations in preS1 of a large envelop protein of HBV may have profound implications in HBV receptor binding to hepatocytes and subsequent entry of the virus into host cells. Aims: This study aimed to identify the mutations in preS1 region and the receptor binding interactions of preS1 with hepatocytes. Methods: The mutations were searched through direct sequencing of the preS1 region. Sequence analysis was done through ClustalX and Jalview. Ab initio modeling of preS1 was done through Rosetta and QUARK followed by glycosylation of best model of preS1. Finally the interactions of preS1 with ASGPR was studied using PatchDock and analysis was done using MOE and pyMol. Results: Sequence comparison revealed changes in the preS1 region. Ab initio modeling results showed that preS1 is an overall unstructured protein with the presence of three structural motifs. Docking of preS1 with asialoglycoprotein receptor showed mostly hydrophobic interactions. Conclusion: In conclusion, preS1 sequences from Pakistani isolates were found to be 90% conserved and the predicted structure of preS1 was near to native structure.
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