English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Semisynthesis of functional glycosylphosphatidylinositol-anchored proteins

Roller, R., Malik, A., Carillo, M. A., Garg, M., Rella, A., Raulf, M.-K., et al. (2020). Semisynthesis of functional glycosylphosphatidylinositol-anchored proteins. Angewandte Chemie International Edition, 59(29), 12035-12040. doi:10.1002/anie.202002479.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/21.11116/0000-0006-3F29-7 Version Permalink: http://hdl.handle.net/21.11116/0000-0006-C3A0-8
Genre: Journal Article

Files

show Files
hide Files
:
Article.pdf (Publisher version), 2MB
Name:
Article.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-

Locators

show

Creators

show
hide
 Creators:
Roller, Renée1, Author              
Malik, Ankita1, Author              
Carillo, Maria Antonietta1, Author              
Garg, Monika1, Author              
Rella, Antonella1, Author              
Raulf, Marie-Kristin, Author
Lepenies, Bernd, Author
Seeberger, Peter H.2, Author              
Varón Silva, Daniel1, Author              
Affiliations:
1Daniel Varón Silva, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863302              
2Peter H. Seeberger, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_2040285              

Content

show
hide
Free keywords: GPI anchor; glycoproteins; glypiation; protein modifications; protein semisynthesis
 Abstract: Glypiation is a common posttranslational modification of eukaryotic proteins involving the attachment of a glycosylphosphatidylinositol (GPI) glycolipid. GPIs contains a conserved phosphoglycan modified in cell- and tissue-specific manner. GPI complexity suggests roles in biological processes and effects on the attached proteins, but the difficulties to get homogeneous material hinder the studies. Here, we disclose a one-pot intein-mediated ligation (OPL) to obtain GPI-anchored proteins. The strategy allows for glypiation of folded and denatured proteins with a natural linkage to the glycolipid. Using the strategy, glypiated eGFP, Thy1, and the Plasmodium berghei MSP119 were prepared. Glypiation did not alter the structure of eGFP and MSP119 proteins in solution, but it induced a strong pro-inflammatory response in vitro. The strategy provides access to glypiated proteins to elucidate the activity of this modification and for use as vaccine candidates against parasitic infections.

Details

show
hide
Language(s): eng - English
 Dates: 2020-04-192020
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Angewandte Chemie International Edition
  Abbreviation : Angew. Chem., Int. Ed.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Weinheim : Wiley-VCH
Pages: - Volume / Issue: 59 (29) Sequence Number: - Start / End Page: 12035 - 12040 Identifier: ISSN: 1433-7851

Source 2

show
hide
Title: Angewandte Chemie
  Abbreviation : Angew. Chem.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Weinheim : Wiley-VCH
Pages: - Volume / Issue: 132 (29) Sequence Number: - Start / End Page: 12133 - 12138 Identifier: ISSN: 0044-8249