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Bead Loading Proteins and Nucleic Acids into Adherent Human Cells
Published on: June 1, 2021
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Carb loading takes proteins on a ride
Christina Schäffer1, Paul Messner2
1From the Department of NanoBiotechnology, NanoGlycobiology Unit, Universität für Bodenkultur Wien, A-1190 Vienna, Austria christina.schaeffer@boku.ac.at.
The Journal of Biological Chemistry
|April 8, 2018
Summary
Bacterial protein export relies on O-glycosylation, a modification essential for protein maturation. This study reveals how glycosyltransferases and translocation systems work together to deliver modified adhesins to the membrane.
Area of Science:
- Microbiology
- Molecular Biology
- Biochemistry
Background:
- Bacterial protein O-glycosylation is crucial for protein maturation.
- The role of carbohydrate modifications in bacterial protein export is not well understood.
Purpose of the Study:
- To elucidate the mechanism of posttranslational modification of a Streptococcus gordonii adhesin.
- To develop a comprehensive model for the interplay of glycosyltransferases and the translocation system in bacterial protein export.
Main Methods:
- Investigated the posttranslational modification of a specific Streptococcus gordonii adhesin.
- Analyzed the interaction between glycosyltransferases and the protein translocation system.
Main Results:
- Described the mechanism for O-glycosylation of a Streptococcus gordonii adhesin.
- Provided the first comprehensive model detailing the interplay of glycosyltransferases and the translocation system for protein delivery to the membrane.
Conclusions:
- Bacterial protein export is dependent on O-glycosylation.
- A novel model highlights the coordinated function of glycosyltransferases and translocation systems in bacterial adhesin delivery.
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