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

Author Correction: Discovery of indole-modified aptamers for highly specific recognition of protein glycoforms
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DOI:
10.1101/2021.03.13.435263
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发表时间:
2021-03
影响因子:
16.6
通讯作者:
A. Yoshikawa;Alexandra E. Rangel;T. Feagin;E. M. Chun;Leighton Wan;Anping Li;Leonhard Moeckl;D. Wu;M. Eisenstein;Sharon J. Pitteri;H. Soh
A. Yoshikawa;Alexandra E. Rangel;T. Feagin;E. M. Chun;Leighton Wan;Anping Li;Leonhard Moeckl;D. Wu;M. Eisenstein;Sharon J. Pitteri;H. Soh
中科院分区:
综合性期刊1区
文献类型:
--
作者:
A. Yoshikawa;Alexandra E. Rangel;T. Feagin;E. M. Chun;Leighton Wan;Anping Li;Leonhard Moeckl;D. Wu;M. Eisenstein;Sharon J. Pitteri;H. Soh

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糖基化是最丰富的翻译后修饰形式之一,可以对广泛的生物过程和疾病产生深远的影响。不幸的是,由于缺乏可以区分蛋白质糖型的亲和试剂,在基础和临床研究中表征此类修饰的努力受到严重阻碍。试剂的缺乏很大程度上是由于与生成能够以强大的亲和力和特异性结合特定聚糖表位的亲和试剂相关的挑战。在这项工作中,我们使用基于荧光激活细胞分选(FACS)的方法来生成和筛选具有吲哚修饰碱基的适体,以努力分离可以区分蛋白质糖型的试剂。使用这种方法,我们能够选择多个适体,这些适体对两种不同蛋白质的特定糖型表现出很强的选择性,并且能够区分具有相同三级结构的分子,这些分子仅在聚糖修饰方面有所不同。
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 such modifications in the context of basic and clinical research are severely hampered by the lack of affinity reagents that can differentiate protein glycoforms. This lack of reagents is largely due to the challenges associated with generating affinity reagents that can bind to particular glycan epitopes 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 in an effort to isolate reagents that can differentiate between protein glycoforms. Using this approach, we were able to select multiple aptamers that exhibit strong selectivity for specific glycoforms of two different proteins, with the capacity to discriminate between molecules with identical tertiary structures that differ only in terms of their glycan modifications.