Semisynthesis of Functional Glycosylphosphatidylinositol-Anchored Proteins.
GPI anchor
glycoproteins
glypiation
protein modifications
protein semisynthesis
Journal
Angewandte Chemie (International ed. in English)
ISSN: 1521-3773
Titre abrégé: Angew Chem Int Ed Engl
Pays: Germany
ID NLM: 0370543
Informations de publication
Date de publication:
13 07 2020
13 07 2020
Historique:
received:
17
02
2020
revised:
30
03
2020
pubmed:
21
4
2020
medline:
26
3
2021
entrez:
21
4
2020
Statut:
ppublish
Résumé
Glypiation is a common posttranslational modification of eukaryotic proteins involving the attachment of a glycosylphosphatidylinositol (GPI) glycolipid. GPIs contain a conserved phosphoglycan that is modified in a cell- and tissue-specific manner. GPI complexity suggests roles in biological processes and effects on the attached protein, but the difficulties to get homogeneous material have hindered studies. We disclose a one-pot intein-mediated ligation (OPL) to obtain GPI-anchored proteins. The strategy enables the glypiation of folded and denatured proteins with a natural linkage to the glycolipid. Using the strategy, glypiated eGFP, Thy1, and the Plasmodium berghei protein MSP1
Identifiants
pubmed: 32307806
doi: 10.1002/anie.202002479
pmc: PMC7383966
doi:
Substances chimiques
Bacterial Proteins
0
Bacterial Vaccines
0
Glycolipids
0
Glycosylphosphatidylinositols
0
Membrane Proteins
0
Green Fluorescent Proteins
147336-22-9
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
12035-12040Informations de copyright
© 2020 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA.
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