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VERSION:2.0
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BEGIN:VEVENT
DTSTAMP:20260607T013059Z
UID:https://www.mr.mpg.de/events/16897/10694
DTSTART:20191104T150000Z
DTEND:20191104T160000Z
CLASS:PUBLIC
CREATED:20181130T061346Z
DESCRIPTION: Complex multistep biosynthetic pathways that afford asparagine
 -linked (N-linked) glycoproteins occur in all domains of life. The extreme
 ly varied and critical functions of N-linked glycosylation in mammalian bi
 ology makes this process of significant importance in human health and dis
 ease 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 imp
 ortant 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\, prokar
 yotic N-linked glycoproteins integrate a far greater diversity of carbohyd
 rate building blocks and glycosidic linkages\, relative to their eukaryoti
 c 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 produc
 ed through membrane-associated pathways are implicated in host-pathogen in
 teractions and are displayed on bacterial cell surfaces as virulence facto
 rs. 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 id
 entities 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 con
 trast the structures and functions of key enzymes in the N-glycosylation p
 athways across domains of life and highlight enzymatic steps in Gram-negat
 ive pathogens that are critical for virulence and pathogenicity in human h
 osts. In addition\, I will present approaches for investigation of multien
 zyme complexes in liponanoparticles ultimately targeted at understanding t
 he role of lipids in protein-protein interactions at membrane interfaces.
LAST-MODIFIED:20191017T071308Z
LOCATION:MPI for Medical Research\, Room: Seminar Room A/B
ORGANIZER;CN=MPI for Medical Research:mailto:pr@mpimf-heidelberg.mpg.de
SUMMARY:Rudolf Mößbauer Colloquium with Barbara Imperiali (MIT) - Protein
  glycosylation: pathways and processes: Rudolf Mößbauer Colloquium with 
 Barbara Imperiali (MIT) - Protein glycosylation: pathways and processes
URL;VALUE=URI:https://www.mr.mpg.de/events/16897/10694
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