- Research Assistant Professor, University of Notre Dame
- Research Scientist, University of Notre Dame
- Research Associate, The Rockefeller University
- Postdoctoral Associate, The Rockefeller University
- Ph.D. in Biochemistry, University of Notre Dame
- M.S. in Biology, Chonnam National University, Korea
- B.S. in Genetic Engineering, Chonnam National University, Korea
Methicillin-resistant Staphylococcus aureus (MRSA) is a nefarious human pathogen. It causes both hospital-acquired (HA-MRSA) and community-acquired (CA-MRSA) infections. MRSA kills approximately 11,000 individuals annually in the United States alone. About 80% of MRSA bacteria harbor a bla operon that consists of two regulatory genes, blaR1 and blaI, and a structural gene blaZ encoding a class A β-lactamase (BlaZ), a resistant determinant for β-lactam antibiotics. Dr. Kim recently identified for the first time that the staphylococcal BlaZ exists in two forms, one phosphorylated and another not phosphorylated. A remarkable feature of this discovery is that when the protein is phosphorylated, it is sequestered exclusively to the bacterial membrane by lipidation, whereas the non-phosphorylated form is excreted to the milieu. An intriguing observation pointed to the potential involvement of BlaZ in staphylococcal virulence. When the blaZ was removed from MRSA, it exhibited an increase of opsonophagocytic killing by neutrophil cells as well as a decrease in deposition of the complementary protein C3b.
Dr. Kimâs research focuses on the elucidation of the pathways that inhibition of phosphorylation of BlaZ would target for release from the S. aureus surface, leading to its loss as a virulence factor for the bacterium. We expect that our identification of the kinase(s) phosphorylating BlaZ will make it a target for inhibition that converts virulent strains to avirulent ones.
- Choi, Y.; Park, J. S.; Kim, J.; Min, K.; Mahasenan, K.; Kim, C.; Yoon, H. J.; Lim, S.; Cheon, D. H.; Lee, Y.; Ryu, S.; Mobashery, S.; Kim, B. M. and Lee, H. H. "Structure-Based Inhibitor Design for Reshaping Bacterial Morphology" 2022 Communications Biology, 5 (1), 395. DOI: 10.1038/s42003-022-03355-3.
- Martinez-Caballero, S.; Mahasenan, K. V.; Kim, C.; Molina, R.; Feltzer, R.; Lee, M.; Bouley, R.; Hesek, D.; Fisher, J. F.; Munoz, I. G.; Chang, M.; Mobashery, S. and Hermoso, J. A. "Integrative Structural Biology of the Penicillin-Binding Protein-1 from Staphylococcus Aureus, an Essential Component of the Divisome Machinery" 2021 Computational and Structural Biotechnology Journal, 19, pp.5392-5405. DOI: 10.1016/j.csbj.2021.09.018.
- Kim, C.; Mahasenan, K. V.; Bhardwaj, A.; Wiest, O.; Chang, M. and Mobashery, S. "Production of Proteins of the SARS-CoV-2 Proteome for Drug Discovery" 2021 ACS Omega, 6 (30), pp.19983-19994. DOI: 10.1021/acsomega.1c02984.
- Dik, D. A.; Kim, C.; Madukoma, C. S.; Fisher, J. F.; Shrout, J. D. and Mobashery, S. "Fluorescence Assessment of the AmpR-Signaling Network of Pseudomonas Aeruginosa to Exposure to Beta-Lactam Antibiotics" 2020 ACS Chemical Biology, 15 (5), pp.1184-1194. DOI: 10.1021/acschembio.9b00875.
- Mahasenan, K. V.; Batuecas, M. T.; De Benedetti, S.; Kim, C.; Rana, N.; Lee, M.; Hesek, D.; Fisher, J. F.; Sanz-Aparicio, J.; Hermoso, J. A. and Mobashery, S. "Catalytic Cycle of Glycoside Hydrolase BglX from Pseudomonas Aeruginosa and its Implications for Biofilm Formation" 2020 ACS Chemical Biology, 15 (1), pp.189-196. DOI: 10.1021/acschembio.9b00754.
- Ceballos, S.; Kim, C.; Qian, Y. Y.; Mobashery, S.; Chang, M. and Torres, C. "Susceptibility of Methicillin-Resistant Staphylococcus Aureus to Five Quinazolinone Antibacterials" 2020 Antimicrobial Agents and Chemotherapy, 64 (1), e01344-19. DOI: 10.1128/AAC.01344-19.