Rudolf Mößbauer Colloquium with Barbara Imperiali (MIT) - Protein glycosylation: pathways and processes

Rudolf Mößbauer Colloquium with Barbara Imperiali (MIT) - Protein glycosylation: pathways and processes

  • Date: Nov 4, 2019
  • Time: 16:00 - 17:00
  • Location: MPI for Medical Research
  • Room: Seminar Room A/B
  • Host: MPI for Medical Research
  • Contact: pr@mpimf-heidelberg.mpg.de
Rudolf Mößbauer Colloquium with Barbara Imperiali (MIT) - Protein glycosylation: pathways and processes
Complex multistep biosynthetic pathways that afford asparagine-linked (N-linked) glycoproteins occur in all domains of life. The extremely varied and critical functions of N-linked glycosylation in mammalian biology makes this process of significant importance in human health and disease and also of great relevance in medicine and biotechnology as protein therapeutics have become important elements in the modern pharmacopoeia. N-linked glycosylation also occurs in prokaryotes, and, although many important details remain to be explored, it is now clear that there are key differences between the pathways and the resultant glycoprotein functions relative to the well-understood eukaryotic processes. For example, prokaryotic N-linked glycoproteins integrate a far greater diversity of carbohydrate building blocks and glycosidic linkages, relative to their eukaryotic counterparts. Therefore, there is considerable interest the development of chemical biology tools to provide insight into this phenomenon and its functional consequences. In this context, bacterial glycoproteins produced through membrane-associated pathways are implicated in host-pathogen interactions and are displayed on bacterial cell surfaces as virulence factors. Additionally, while multistep N-linked protein glycosylation pathways characterized to date feature glycan assembly at the bilayer interface on linear polyprenol phosphates, there are intriguing differences in the identities of the polyprenols and the physical and biological roles of these unusual terpenes. This presentation will discuss themes reflected in our current research on N-linked protein glycosylation. I will compare and contrast the structures and functions of key enzymes in the N-glycosylation pathways across domains of life and highlight enzymatic steps in Gram-negative pathogens that are critical for virulence and pathogenicity in human hosts. In addition, I will present approaches for investigation of multienzyme complexes in liponanoparticles ultimately targeted at understanding the role of lipids in protein-protein interactions at membrane interfaces.
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