Structure and dynamics of an α-fucosidase reveal a mechanism for highly efficient IgG transfucosylation

Erik H. Klontz; Chao Li; Kyle Kihn; James K. Fields; Dorothy Beckett; Greg A. Snyder; Patrick L. Wintrode; Daniel Deredge; Lai-Xi Wang; Eric J. Sundberg

doi:10.1038/s41467-020-20044-z

Nature Communications (Dec 2020)

Structure and dynamics of an α-fucosidase reveal a mechanism for highly efficient IgG transfucosylation

Erik H. Klontz,
Chao Li,
Kyle Kihn,
James K. Fields,
Dorothy Beckett,
Greg A. Snyder,
Patrick L. Wintrode,
Daniel Deredge,
Lai-Xi Wang,
Eric J. Sundberg

Affiliations

Erik H. Klontz: Institute of Human Virology, University of Maryland School of Medicine
Chao Li: Department of Chemistry and Biochemistry, University of Maryland
Kyle Kihn: Department of Pharmaceutical Sciences, University of Maryland School of Pharmacy
James K. Fields: Institute of Human Virology, University of Maryland School of Medicine
Dorothy Beckett: Department of Chemistry and Biochemistry, University of Maryland
Greg A. Snyder: Institute of Human Virology, University of Maryland School of Medicine
Patrick L. Wintrode: Department of Pharmaceutical Sciences, University of Maryland School of Pharmacy
Daniel Deredge: Department of Pharmaceutical Sciences, University of Maryland School of Pharmacy
Lai-Xi Wang: Department of Chemistry and Biochemistry, University of Maryland
Eric J. Sundberg: Institute of Human Virology, University of Maryland School of Medicine

DOI: https://doi.org/10.1038/s41467-020-20044-z
Journal volume & issue: Vol. 11, no. 1
pp. 1 – 14

Abstract

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AlfC transfucosidase is used to modulate fucosylation of glycans decorating monoclonal antibodies. Herein, structural and biophysical characterization reveals the enzymatic mechanism of AlfC and a blueprint for the design of AlfC mutants with novel specificities and functions.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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