Characterization and structural analysis of Iranian Human Papilloma Viruses L1 Protein

Abstract

HPV is a small, non-enveloped DNA virus that is related to human cervical cancer. The HPV genome encodes six characterized proteins. L1 is the major part of the current vaccines and any changes in this region can be followed by a decrease in vaccine efficiency. The aim of this research was comparison analysis among Iranian L1 protein sequences with reference sequences to determine the possible substation in this region; in addition, finding L1 physicochemical and structural properties by using bioinformatics tools to provide comprehensive comprehension of HPV L1 protein. 13 Iranian PV sequences L1 protein and reference sequences were selected and obtained from NCBI data bank. “CLC sequence viewer” was used to translate the alignment. To predict the signal peptide, “predisi”, and “phobius” were employed. Secondary and tertiary structure and structure validation of all sequences were analyzed.Findings showed that L1 is highly conserved and just two mutations were found in this region. No signal peptide was described and the main part of this region included the random coil. Tertiary structure by different software was mapped and 5 distinct loops were found. This study is the first report that investigated the change in the L1 protein of Iranian patients and provided practical comprehension of L1 properties that is vital for cloning and producing the new generation of virus-like particles (VLPs) vaccines. Furthermore, the structural analysis showed several loops that had an indispensable role in antibody binding and the prevention of HPV infections.

Keywords

• hpv
• in silico
• l1
• structural analysis
• physicochemical properties
• bioinformatics