Labroots’ virtual events are a fantastic way to network and learn about the work of other researchers in your field. These events feature participants from around the world who can showcase their research for free in a virtual poster format. At this year’s Microbiology Virtual Week (now available to view On-Demand), Labroots highlighted an exceptional study involving the fight against tuberculosis (TB). This distinctive work comes from Dr. Emmanuel Ogbonna, a Postdoctoral Research Fellow at Harvard Medical School, but the research itself was conducted when he was still a PhD student at the University of Delaware.
(To see the full poster in detail, check out the 2022 Microbiology Virtual Week On-Demand)
Ogbonna’s poster examined how the ATP-dependent protease ClpC1P1P2 is the target for new drug techniques, specifically against multi-drug resistant Mycobacterium tuberculosis (Mtb). The findings include new evidence that reinforces the presence of phosphoarginine-mediated proteolysis by the ATP-dependent protease ClpC1P1P2 in mycobacteria and other species of actinobacteria.
Ogbonna told Labroots that the most meaningful result of the project was the potential of N-methylhydantoinase to influence both ATPase and peptidase stimulatory pursuits of ClpC1. Ogbonna notes that the multi-pronged outcome strongly advocates that the modulation/regulation is built on configuration change.
“The goal of my research is to develop novel drugs against TB,” Ogbonna said. “So, a regulator like Nmh which almost completely shuts off an enzyme (ClpC1P1P2 protease) essential for the pathogen's viability presents an avenue for the development of synthetic mimics (e.g peptides) to target the pathogen.”
As a Postdoctoral Research Fellow at Harvard Medical School, Ogbonna continues his studies into TB progression, albeit from a tissue pathology vantage point using multiplex imaging techniques and single cell phenotyping.
The full manuscript for this project is currently in review but can be viewed now on bioRxiv. To follow Dr. Ogbonna’s research and career, and to connect with him, check out his LinkedIn page.
