Discovery of indole-modified aptamers for highly specific recognition of protein glycoforms

Alex M. Yoshikawa, Alexandra Rangel, Trevor Feagin, Elizabeth M. Chun, Leighton Wan, Anping Li, Leonhard Moeckl, Diana Wu, Michael Eisenstein, Sharon Pitteri and H. Tom Soh ()
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Alex M. Yoshikawa: Stanford University
Alexandra Rangel: Stanford University
Trevor Feagin: Stanford University
Elizabeth M. Chun: Stanford University
Leighton Wan: Stanford University
Anping Li: Stanford University
Leonhard Moeckl: Stanford University
Diana Wu: Stanford University
Michael Eisenstein: Stanford University
Sharon Pitteri: Stanford University
H. Tom Soh: Stanford University

Nature Communications, 2021, vol. 12, issue 1, 1-12

Abstract: Abstract Glycosylation is one of the most abundant forms of post-translational modification, and can have a profound impact on a wide range of biological processes and diseases. Unfortunately, efforts to characterize the biological function of such modifications have been greatly hampered by the lack of affinity reagents that can differentiate protein glycoforms with robust affinity and specificity. In this work, we use a fluorescence-activated cell sorting (FACS)-based approach to generate and screen aptamers with indole-modified bases, which are capable of recognizing and differentiating between specific protein glycoforms. Using this approach, we were able to select base-modified aptamers that exhibit strong selectivity for specific glycoforms of two different proteins. These aptamers can discriminate between molecules that differ only in their glycan modifications, and can also be used to label glycoproteins on the surface of cultured cells. We believe our strategy should offer a generally-applicable approach for developing useful reagents for glycobiology research.

Date: 2021
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DOI: 10.1038/s41467-021-26933-1

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