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Engineered High‐Specificity Affinity Reagents for the Detection of Glycan Sialylation
Author(s) -
Woods Robert J.,
Wu Shengcheng,
Meng Lu,
GernerSmidt Christian,
Sanders Matthew J.,
BenAyre Shani Leviatan,
PadlerKaravani Vered,
Yang Loretta
Publication year - 2019
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2019.33.1_supplement.801.2
Subject(s) - glycan , sialic acid , sialidase , enzyme , biochemistry , lectin , chemistry , affinity chromatography , reagent , glycoprotein , computational biology , western blot , microbiology and biotechnology , biology , neuraminidase , gene
As alternatives to established carbohydrate‐detection reagents (antibodies and lectins), Lectenz ® Bio is developing lectin‐like, enzyme‐derived proteins (known as Lectenz ® ), that target glycan sequences for which existing reagents either do not exist or are sub‐optimal. Lectenz ® are engineered from catalytically inactivated glycan‐processing enzymes that have been optimized for high affinity towards specific glycan sequences. The conversion of such enzymes into affinity reagents is facilitated by computationally‐guided directed evolution. Lectenz ® are being developed for a variety of glycan detection and enrichment applications including affinity chromatography, Western blot, and immunohistochemistry. Here we demonstrate the performance and specificity of two novel sialic acid recognizing Lectenz ® engineered from a sialidase enzyme. Support or Funding Information NIH R44 GM113351, R44 OD024964 This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .