Reception at 3 pm.

Reception at 3 pm.

Reception at 3 pm.

Reception at 3 pm.

Reception at 3 pm.

Reception at 3 pm.

Reception at 3 pm.

Refreshments will be served at 10:00am.
Attendance will be taken at the conclusion of the presentation.

Carbohydrates add a level of diversity across all forms of life that is unparalleled by the information content of nucleic acids and proteins. The lack of a simple template to translate aglycan code into defined sugar structures contributes to this complexity and provides a challenge for efforts aimed at the production of biologically important glycans and glycoconjugates. With the discovery of glycoprotein synthesis in bacteria and functional transfer of glycosylation pathways between species, Escherichia coli cells have become a tractable host for understanding glycosylation and the underlying glycan code of living cells. Moreover, efforts to manipulate the pathways from sugar nucleotides to glycolipids to glycoproteins have transformed E. coli into a living factory for scalable, bottom-up production of complex glycoconjugates by design. Here, I will discuss our efforts to develop E. coli for the biosynthesis of a diverse array of glycan structures, which can be used to tailor the activity, stability, half-life, and immunogenicity of a given biopharmaceutical. I will also discuss our efforts to unify protein glycosylation in E. coli with the advanced tools of protein engineering such as cell surface and phage display technologies. The result is a powerful new way to engineer the enzymes, pathways, end-products, and genomes of glycoengineered bacteria for creating the next generation of protein therapeutics and vaccines for a wide range of human diseases.

Matthew P. DeLisa is the William L. Lewis Professor of Engineering in the School of Chemical and Biomolecular Engineering at Cornell University. His research focuses on understanding and controlling the molecular mechanisms underlying protein biogenesis – folding and assembly, membrane translocation and post-translational modifications – in the complex environment of a living cell. Professor DeLisa received a B.S. in Chemical Engineering from the University of Connecticut in 1996; a Ph.D. in Chemical Engineering from the University of Maryland in 2001; and did postdoctoral work at the University of Texas-Austin, Department of Chemical Engineering. DeLisa joined the Department of Chemical and Biomolecular Engineering at Cornell University in 2003. He has also served as a Gastprofessur at the Swiss Federal Institute of Technology (ETH Zürich) in the Institut für Mikrobiologie.

Refreshments will be served at 10:00am.
Attendance will be taken at the conclusion of the presentation.

Universal O2-carrying solutions that can replace the O2 storage and transport functions of red blood cells (RBCs) will greatly improve clinical outcomes for trauma victims and patients undergoing high-blood-loss surgical procedures. These O2 carriers are to be used when blood is not readily available, such as on the battlefield, during natural disasters, at the site of a terrorist attack or in rural areas without hospital access. My talk will address a simple approach for designing hemoglobin-based O2 carriers (HBOCs) as RBC substitutes. Our design strategy is based on the observation that transfusion of cell-free hemoglobin results in vasoconstriction, systemic hypertension and oxidative tissue injury. The root cause of these side-effects stem from the ability of hemoglobin to extravasate through pores lining the wall of blood vessels, and consequently scavenge nitric oxide from the surrounding vasculature as well as catalyze production of reactive oxygen species. Therefore, our design strategy will focus on increasing the molecular diameter of HBOCs so that they are unable to traverse across the wall of blood vessels into the tissue space to limit/prevent these side-effects. In this talk, I will discuss the design, biophysical properties and in vivo response of polymerized hemoglobin (a class of HBOC).

Professor Palmer is author of more than 100 peer reviewed publications. Among others, he received the National Science Foundation Career Award, and the Harrison Faculty Award for Excellence in Engineering Education from The Ohio State University College of Engineering. Prof. Palmer currently serves on the International Scientific Advisory Committee on Blood Substitutes, and is a member of the Bioengineering, Technology, and Surgical Sciences Study Section at the National Institutes of Health. In 2015, he was inducted into the College of Fellows of the American Institute for Medical and Biological Engineering, and appointed chair of the William G. Lowrie Department of Chemical Engineering at The Ohio State University. Palmer’s research is supported by grants from the National Institutes of Health and the Department of Defense.

Refreshments will be served at 10:00am.
Attendance taken at the conclusion of the presentation.