Glycotope structures and intramolecular affinity factors of plant lectins for Tn/T antigens

Pierre Rougé; Willy J. Peumans; Els J.M. Van Damme; Annick Barre; Tanuja Singh; June H. Wu; Albert M. Wu

doi:10.1007/978-1-4419-7877-6_8

Glycotope structures and intramolecular affinity factors of plant lectins for Tn/T antigens

Pierre Rougé^*, Willy J. Peumans, Els J.M. Van Damme, Annick Barre, Tanuja Singh, June H. Wu, Albert M. Wu

^*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceeding › Conference contribution › peer-review

6 Scopus citations

Abstract

O-glycosylation is a widely distributed posttranslational modification initiated by the addition of GalNAc to serine or threonine residues of polypeptide chains. The GalNAc may be further substituted to form linear/branched sugar chains. Some proteins, like the mucins of vertebrates, are extensively O-glycosylated and consist predominantly of carbohydrate. T antigens, which were originally designated as Thomsen-Friedenreich or TF antigens, are of particular interest in glycobiology since a high expression of the T antigen on the cell surface can be used as a glycomarker [1-3]. Due to the apparent loss of βGalactosyl-transferase, which normally converts the Tn antigen (GalNAcα1-Thr/Ser) into the T antigen (Galβ1,3GalNAcα1- Thr/Ser), the precursor Tn antigen accumulates in cancer cells (Fig. 8.1).

Original language	English
Title of host publication	The Molecular Immunology of Complex Carbohydrates-3
Editors	Albert Wu
Pages	143-154
Number of pages	12
DOIs	https://doi.org/10.1007/978-1-4419-7877-6_8
State	Published - 2011
Externally published	Yes

Publication series

Name	Advances in Experimental Medicine and Biology
Volume	705
ISSN (Print)	0065-2598

Keywords

Glycosylation
Plant lectins
T glycotope
Tn glycotope

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1007/978-1-4419-7877-6_8

Cite this

Rougé, P., Peumans, W. J., Van Damme, E. J. M., Barre, A., Singh, T., Wu, J. H., & Wu, A. M. (2011). Glycotope structures and intramolecular affinity factors of plant lectins for Tn/T antigens. In A. Wu (Ed.), The Molecular Immunology of Complex Carbohydrates-3 (pp. 143-154). (Advances in Experimental Medicine and Biology; Vol. 705). https://doi.org/10.1007/978-1-4419-7877-6_8

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abstract = "O-glycosylation is a widely distributed posttranslational modification initiated by the addition of GalNAc to serine or threonine residues of polypeptide chains. The GalNAc may be further substituted to form linear/branched sugar chains. Some proteins, like the mucins of vertebrates, are extensively O-glycosylated and consist predominantly of carbohydrate. T antigens, which were originally designated as Thomsen-Friedenreich or TF antigens, are of particular interest in glycobiology since a high expression of the T antigen on the cell surface can be used as a glycomarker [1-3]. Due to the apparent loss of βGalactosyl-transferase, which normally converts the Tn antigen (GalNAcα1-Thr/Ser) into the T antigen (Galβ1,3GalNAcα1- Thr/Ser), the precursor Tn antigen accumulates in cancer cells (Fig. 8.1).",

keywords = "Glycosylation, Plant lectins, T glycotope, Tn glycotope",

author = "Pierre Roug{\'e} and Peumans, {Willy J.} and {Van Damme}, {Els J.M.} and Annick Barre and Tanuja Singh and Wu, {June H.} and Wu, {Albert M.}",

year = "2011",

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Glycotope structures and intramolecular affinity factors of plant lectins for Tn/T antigens. / Rougé, Pierre; Peumans, Willy J.; Van Damme, Els J.M. et al.
The Molecular Immunology of Complex Carbohydrates-3. ed. / Albert Wu. 2011. p. 143-154 (Advances in Experimental Medicine and Biology; Vol. 705).

Research output: Chapter in Book/Report/Conference proceeding › Conference contribution › peer-review

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AU - Peumans, Willy J.

AU - Van Damme, Els J.M.

AU - Barre, Annick

AU - Singh, Tanuja

AU - Wu, June H.

AU - Wu, Albert M.

PY - 2011

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N2 - O-glycosylation is a widely distributed posttranslational modification initiated by the addition of GalNAc to serine or threonine residues of polypeptide chains. The GalNAc may be further substituted to form linear/branched sugar chains. Some proteins, like the mucins of vertebrates, are extensively O-glycosylated and consist predominantly of carbohydrate. T antigens, which were originally designated as Thomsen-Friedenreich or TF antigens, are of particular interest in glycobiology since a high expression of the T antigen on the cell surface can be used as a glycomarker [1-3]. Due to the apparent loss of βGalactosyl-transferase, which normally converts the Tn antigen (GalNAcα1-Thr/Ser) into the T antigen (Galβ1,3GalNAcα1- Thr/Ser), the precursor Tn antigen accumulates in cancer cells (Fig. 8.1).

AB - O-glycosylation is a widely distributed posttranslational modification initiated by the addition of GalNAc to serine or threonine residues of polypeptide chains. The GalNAc may be further substituted to form linear/branched sugar chains. Some proteins, like the mucins of vertebrates, are extensively O-glycosylated and consist predominantly of carbohydrate. T antigens, which were originally designated as Thomsen-Friedenreich or TF antigens, are of particular interest in glycobiology since a high expression of the T antigen on the cell surface can be used as a glycomarker [1-3]. Due to the apparent loss of βGalactosyl-transferase, which normally converts the Tn antigen (GalNAcα1-Thr/Ser) into the T antigen (Galβ1,3GalNAcα1- Thr/Ser), the precursor Tn antigen accumulates in cancer cells (Fig. 8.1).

KW - Glycosylation

KW - Plant lectins

KW - T glycotope

KW - Tn glycotope

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Glycotope structures and intramolecular affinity factors of plant lectins for Tn/T antigens

Abstract

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Keywords

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