| Literature DB >> 33958792 |
Mirat Sojitra1, Susmita Sarkar1, Jasmine Maghera1, Emily Rodrigues1, Eric J Carpenter1, Shaurya Seth1, Daniel Ferrer Vinals1, Nicholas J Bennett1, Revathi Reddy1, Amira Khalil1,2, Xiaochao Xue1, Michael R Bell1, Ruixiang Blake Zheng1, Ping Zhang3, Corwin Nycholat4, Justin J Bailey1, Chang-Chun Ling3, Todd L Lowary1,5,6, James C Paulson4, Matthew S Macauley1,7, Ratmir Derda8.
Abstract
The central dogma of biology does not allow for the study of glycans using DNA sequencing. We report a liquid glycan array (LiGA) platform comprising a library of DNA 'barcoded' M13 virions that display 30-1,500 copies of glycans per phage. A LiGA is synthesized by acylation of the phage pVIII protein with a dibenzocyclooctyne, followed by ligation of azido-modified glycans. Pulldown of the LiGA with lectins followed by deep sequencing of the barcodes in the bound phage decodes the optimal structure and density of the recognized glycans. The LiGA is target agnostic and can measure the glycan-binding profile of lectins, such as CD22, on cells in vitro and immune cells in a live mouse. From a mixture of multivalent glycan probes, LiGAs identify the glycoconjugates with optimal avidity necessary for binding to lectins on living cells in vitro and in vivo.Entities:
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Year: 2021 PMID： 33958792 PMCID： PMC8380037 DOI： 10.1038/s41589-021-00788-5
Source DB: PubMed Journal: Nat Chem Biol ISSN： 1552-4450 Impact factor: 16.174