Shotgun scanning glycomutagenesis: A simple and efficient strategy for constructing and characterizing neoglycoproteins
Abstract
Asparagine-linked ( N -linked) protein glycosylation—the covalent attachment of complex sugars to the nitrogen atom in asparagine side chains—is the most widespread posttranslational modification to proteins and also the most complex. N- glycosylation affects a significant number of cellular proteins and can have profound effects on their most important attributes such as biological activity, chemical solubility, folding and stability, immunogenicity, and serum half-life. Accordingly, the strategic installation of glycans at naïve sites has become an attractive means for endowing proteins with advantageous biological and/or biophysical properties. Here, we describe a glycoprotein engineering strategy that enables systematic investigation of the structural and functional consequences of glycan installation at every position along a protein backbone and provides a new route to bespoke glycoproteins.
Document Details
- Document Type
- Pub Defense Publication
- Publication Date
- Sep 22, 2021
- Source ID
- 10.1073/pnas.2107440118
Entities
People
- Emily C. Cox
- Jason W Labonte
- Jeffrey J. Gray
- Josef Byrne
- Matthew P. DeLisa
- Mingji Li
- Qin Fu
- Sheng Zhang
- Sophia W. Hulbert
- Sudhanshu Shanker
- Thapakorn Jaroentomeechai
- Tyler D Moeller
- Xiaolu Zheng
- İlkay Koçer
Organizations
- Cornell University
- Defense Threat Reduction Agency
- Johns Hopkins University
- National Institute of General Medical Sciences
- National Science Foundation
- Office of the Director
- Yusuf Hamied Department of Chemistry