Published Paper Details:

Abstract Neisseria meningitidis is an obligate, gram-negative, human commensal that is spread from person to person by droplet infection. This bacteria colonises the nasopharyngeal mucosa of human and in due course resulted in bacteremia and finally fatal sepsis. Most of the metabolic enzymes that are involved in various biochemical cycles are found to have many secondary functions such as adhesions, regulators of transcription etc. GAPDH is a glycolytic enzyme which is mainly located in the cytoplasm. In addition to its primary metabolic function, it is observed that GAPDH is present on the surface of several microbial pathogens and invasion of host tissues. Since no structural models are available for GAPDH of N. meningitidis, the present study was performed to explore its structural characteristics. It was recorded that the selected protein GAPDH of N.meningitidis was cytoplasmic, stable and with secondary structural elements such as helix and coils, Ramachandran plot showed that it has 92% of aminoacids in the favourable region. The modeled 3D structure of the query protein was refined and validated for its structural features with Q mean, PROCHECK, ERRAT, and PROTSAV servers. The scores given by all these servers were consistent with the fact that the 3D model predicted had good overall quality. Protein function prediction analysis (PFP) showed that the query protein C6S993 has enzymatic role in glycolysis. Binding site analysis revealed that the protein GAPDH of N.meningitidis has binding sites for NAD. The structural model computed in the present study could be used for a comprehensive understanding of the structural characteristics and moonlighting role of GAPDH of N.meningitidis. Details regarding whether the primary and secondary functions are independent or related need further investigation. This study will pave the way for further systematic analysis towards the identification of targets and potential biomarkers to design specific targets