Lectins and ELLSA as powerful tools for glycoconjugate recognition analyses
Lectins, in combination with our established enzyme-linked lectin sorbent assay (ELLSA) and inhibition study, have been used as powerful tools in many glycoconjugate recognition studies. In this short review, we highlight the following: (i) The recognition profiles of Gal/GalNAc-specific lectins wer...
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| Published in | Glycoconjugate journal Vol. 36; no. 2; pp. 175 - 183 |
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| Main Authors | , |
| Format | Journal Article |
| Language | English |
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Springer US
01.04.2019
Springer Nature B.V |
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| Abstract | Lectins, in combination with our established enzyme-linked lectin sorbent assay (ELLSA) and inhibition study, have been used as powerful tools in many glycoconjugate recognition studies. In this short review, we highlight the following: (i) The recognition profiles of Gal/GalNAc-specific lectins were updated and upgraded. (ii) Based on the cross-specificities of applied lectins, a new classification system was introduced. (iii) Applications of lectins for the detection and identification of
N
-glycan and/or Tn glycotope in glycoconjugates were intergraded. (iv) The polyvalency of the glycotopes in glycans was found to play a critical role in glycan–lectin recognition. This is an unexplored area of glycobiology and one of the most promising directions toward the coming glycoscience transformation. |
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| AbstractList | Lectins, in combination with our established enzyme-linked lectin sorbent assay (ELLSA) and inhibition study, have been used as powerful tools in many glycoconjugate recognition studies. In this short review, we highlight the following: (i) The recognition profiles of Gal/GalNAc-specific lectins were updated and upgraded. (ii) Based on the cross-specificities of applied lectins, a new classification system was introduced. (iii) Applications of lectins for the detection and identification of N-glycan and/or Tn glycotope in glycoconjugates were intergraded. (iv) The polyvalency of the glycotopes in glycans was found to play a critical role in glycan–lectin recognition. This is an unexplored area of glycobiology and one of the most promising directions toward the coming glycoscience transformation. Lectins, in combination with our established enzyme-linked lectin sorbent assay (ELLSA) and inhibition study, have been used as powerful tools in many glycoconjugate recognition studies. In this short review, we highlight the following: (i) The recognition profiles of Gal/GalNAc-specific lectins were updated and upgraded. (ii) Based on the cross-specificities of applied lectins, a new classification system was introduced. (iii) Applications of lectins for the detection and identification of N-glycan and/or Tn glycotope in glycoconjugates were intergraded. (iv) The polyvalency of the glycotopes in glycans was found to play a critical role in glycan-lectin recognition. This is an unexplored area of glycobiology and one of the most promising directions toward the coming glycoscience transformation.Lectins, in combination with our established enzyme-linked lectin sorbent assay (ELLSA) and inhibition study, have been used as powerful tools in many glycoconjugate recognition studies. In this short review, we highlight the following: (i) The recognition profiles of Gal/GalNAc-specific lectins were updated and upgraded. (ii) Based on the cross-specificities of applied lectins, a new classification system was introduced. (iii) Applications of lectins for the detection and identification of N-glycan and/or Tn glycotope in glycoconjugates were intergraded. (iv) The polyvalency of the glycotopes in glycans was found to play a critical role in glycan-lectin recognition. This is an unexplored area of glycobiology and one of the most promising directions toward the coming glycoscience transformation. Lectins, in combination with our established enzyme-linked lectin sorbent assay (ELLSA) and inhibition study, have been used as powerful tools in many glycoconjugate recognition studies. In this short review, we highlight the following: (i) The recognition profiles of Gal/GalNAc-specific lectins were updated and upgraded. (ii) Based on the cross-specificities of applied lectins, a new classification system was introduced. (iii) Applications of lectins for the detection and identification of N -glycan and/or Tn glycotope in glycoconjugates were intergraded. (iv) The polyvalency of the glycotopes in glycans was found to play a critical role in glycan–lectin recognition. This is an unexplored area of glycobiology and one of the most promising directions toward the coming glycoscience transformation. |
| Author | Wu, Albert M. Liu, Jia Hau |
| Author_xml | – sequence: 1 givenname: Albert M. surname: Wu fullname: Wu, Albert M. email: amwu@mail.cgu.edu.tw organization: Glycomics Research Laboratory, Institute of Molecular and Cellular Biology, College of Medicine, Chang-Gung University – sequence: 2 givenname: Jia Hau surname: Liu fullname: Liu, Jia Hau organization: Ta-Cheng Stem Cell Therapy Center, National Taiwan University, Division of Hematology, Department of Internal Medicine, National Taiwan University Hospital |
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| Keywords | Lectin–glycan interactions Glycotopes (epitopes) Glycan recognition Applied lectins Polyvalency of glycotopes |
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| Title | Lectins and ELLSA as powerful tools for glycoconjugate recognition analyses |
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