Nilofer Qureshi was born on July 31, 1947, in Karachi, Sindh, Pakistan, the daughter of Ahmed Hussain A. Kazi, a civil servant and economist, and Ayesha Kazi. Her paternal grandfather, Ali Ahmed S Kazi, was a physician and director of health sciences, instrumental in establishing Liaquat University of Medical & Health Sciences. Her maternal grandfather, Ghulam Nabi Kazi, was the first Director of Public Instruction in Sindh, Pakistan, and played a key role in the region’s educational development. Inspired by her family’s legacy in academia and medicine, Nilofer Qureshi aspired to become a scientist from an early age.
In the late 1970s, Qureshi joined the William S. Middleton Memorial VA Hospital (Veterans Health Administration) full-time as a Research Biochemist, focusing on the mechanisms of bacterial toxins and their role in diseases. She pioneered work on the structure of endotoxins from Salmonella and other bacteria, successfully characterizing lipid A components using novel purification techniques and mass spectrometry. [4]
Her work on monophosphoryl lipid A laid the foundation for its use as a vaccine adjuvant, a FDA approved adjuvant. [5]
Academic
In 1993, Qureshi became an Associate Professor at the University of Wisconsin–Madison, where she taught courses on High-Performance Liquid Chromatography (HPLC) and host-parasite relationships. She also mentored graduate students and postdoctoral fellows. In 2001, Dr. Qureshi was appointed Associate Professor of Basic Medical Sciences, and Director of Molecular and Cellular Immunology at University of Missouri–Kansas City School of Medicine. Five years later, she became a tenured professor, and later took on the role of Director of the Shock/Trauma Research Center. During her tenure, she expanded her research on sepsis, proteasomes, and inflammatory diseases. [6][7]
Biochemistry research
Qureshi's research has focused on the biology of lipopolysaccharides (LPS), proteasomes, and their role in inflammatory processes. Her major contributions include:
Establishing the complete structure of the lipid A moiety of LPS from enterobacterial sources. [8]
Developing monophosphoryl lipid A as an effective vaccine adjuvant. [9]
Characterizing LPS antagonists, such as Rhodobacter sphaeroides diphosphoryl lipid A, which inhibits endotoxin activity. [10]
Investigating the ubiquitin-proteasome pathway in macrophages and its implications for septic shock, diabetes, cancer, and cardiovascular diseases. [11]
Her studies have led to novel therapeutic approaches, including proteasome inhibitors/activators for inflammatory diseases. [12]
Publications
Qureshi has authored over 200 scientific publications and book chapters. Some of her works include:
"Reprogramming of Gene Expression of Key Inflammatory Signaling Pathways in Human Peripheral Blood Mononuclear Cells by Soybean Lectin and Resveratrol" (International Journal of Molecular Sciences, 2022). [13]
"The Proteasome as a Lipopolysaccharide-Binding Protein in Macrophages" (The Journal of Immunology, 2003). [14]
"Toll-like Receptor 4 Imparts Ligand-Specific Recognition of Bacterial Lipopolysaccharide" (The Journal of Clinical Investigation, 2000). [15]
"Position of Ester Groups in the Lipid A Backbone of Lipopolysaccharides from Salmonella typhimurium" (Journal of Biological Chemistry, 1983). [16]
Honors and awards
Qureshi's work has earned her numerous accolades, including:
Outstanding Research Achievement Award (Nowotny Award), International Endotoxin and Innate Immunity Society (2021). [17]
^Qureshi, N.; Perera, P.-Y.; Shen, J.; Zhang, G.; Lenschat, A.; Vogel, Stefanie; Morrison, D. (June 1, 2003). "The proteasome may be an important therapeutic target in Gram-negative sepsis". Shock. 19: 15. doi:10.1097/00024382-200306001-00044.
^Qureshi, N.; Perera, P.Y.; Shen, J.; Zhang, G.; Lenschat, A.; Splitter, G.; Morrison, D.C.; Vogel, S.N. (August 1, 2003). "The proteasome as a lipopolysaccharide-binding protein in macrophages: differential effects of proteasome inhibition on lipopolysaccharide-induced signaling events". The Journal of Immunology. 171 (3): 1515–1525. doi:10.4049/jimmunol.171.3.1515. PMID12874245.
