In silico functional elucidation of uncharacterized proteins of Chlamydia abortus strain LLG

AIM This study reports structural modeling, molecular dynamics profiling of hypothetical proteins in Chlamydia abortus genome database. METHODOLOGY The hypothetical protein sequences were extracted from C. abortus LLG Genome Database for functional elucidation using in silico methods. RESULTS Fifty-one proteins with their roles in defense, binding and transporting other biomolecules were unraveled. Forty-five proteins were found to be nonhomologous to proteins present in hosts infected by C. abortus. Of these, 31 proteins were related to virulence. The structural modeling of two proteins, first, WP_006344020.1 (phosphorylase) and second, WP_006344325.1 (chlamydial protease/proteasome-like activity factor) were accomplished. The conserved active sites necessary for the catalytic function were analyzed. CONCLUSION The finally concluded proteins are envisioned as possible targets for developing drugs to curtail chlamydial infections, however, and should be validated by molecular biological methods.