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Plant lectins targeting O-glycans at the cell surface as tools for cancer diagnosis, orognosis and therapy

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Abstract
Aberrant O-glycans expressed at the surface of cancer cells consist of membrane-tethered glycoproteins (T and Tn antigens) and glycolipids (Lewis a, Lewis x and Forssman antigens). All of these O-glycans have been identified as glyco-markers of interest for the diagnosis and the prognosis of cancer diseases. These epitopes are specifically detected using T/Tn-specific lectins isolated from various plants such as jacalin from Artocarpus integrifola, and fungi such as the Agaricus bisporus lectin. These lectins accommodate T/Tn antigens at the monosaccharide-binding site; residues located in the surrounding extended binding-site of the lectins often participate in the binding of more extended epitopes. Depending on the shape and size of the extended carbohydrate-binding site, their fine sugar-binding specificity towards complex O-glycans readily differs from one lectin to another, resulting in a great diversity in their sugar-recognition capacity. T/Tn-specific lectins have been extensively used for the histochemical detection of cancer cells in biopsies and for the follow up of the cancer progression and evolution. T/Tn-specific lectins also induce a caspase-dependent apoptosis in cancer cells, often associated with a more or less severe inhibition of proliferation. Moreover, they provide another potential source of molecules adapted to the building of photosensitizer-conjugates allowing a specific targeting to cancer cells, for the photodynamic treatment of tumors.
Keywords
HUMAN BREAST-CANCER, RIBOSOME-INACTIVATING PROTEIN, THOMSEN-FRIEDENREICH, ANTIGEN, WHEAT-GERM-AGGLUTININ, CARBOHYDRATE-BINDING SPECIFICITIES, AMARANTHUS-LEUCOCARPUS LECTIN, MUSHROOM AGARICUS-BISPORUS, BAUHINIA-FORFICATA LECTIN, SCLEROTIUM-ROLFSII LECTIN, MOLUCCELLA-LAEVIS, LECTIN, lectin, O-glycosylation, Tn antigen, T antigen, Morniga G, peanut, lectin, cancer, diagnosis, prognosis, photodynamic therapy

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Citation

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MLA
Poiroux, Guillaume, et al. “Plant Lectins Targeting O-Glycans at the Cell Surface as Tools for Cancer Diagnosis, Orognosis and Therapy.” INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, vol. 18, no. 6, 2017, doi:10.3390/ijms18061232.
APA
Poiroux, G., Barre, A., Van Damme, E., Benoist, H., & Rougé, P. (2017). Plant lectins targeting O-glycans at the cell surface as tools for cancer diagnosis, orognosis and therapy. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 18(6). https://doi.org/10.3390/ijms18061232
Chicago author-date
Poiroux, Guillaume, Annick Barre, Els Van Damme, Hervé Benoist, and Pierre Rougé. 2017. “Plant Lectins Targeting O-Glycans at the Cell Surface as Tools for Cancer Diagnosis, Orognosis and Therapy.” INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES 18 (6). https://doi.org/10.3390/ijms18061232.
Chicago author-date (all authors)
Poiroux, Guillaume, Annick Barre, Els Van Damme, Hervé Benoist, and Pierre Rougé. 2017. “Plant Lectins Targeting O-Glycans at the Cell Surface as Tools for Cancer Diagnosis, Orognosis and Therapy.” INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES 18 (6). doi:10.3390/ijms18061232.
Vancouver
1.
Poiroux G, Barre A, Van Damme E, Benoist H, Rougé P. Plant lectins targeting O-glycans at the cell surface as tools for cancer diagnosis, orognosis and therapy. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES. 2017;18(6).
IEEE
[1]
G. Poiroux, A. Barre, E. Van Damme, H. Benoist, and P. Rougé, “Plant lectins targeting O-glycans at the cell surface as tools for cancer diagnosis, orognosis and therapy,” INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, vol. 18, no. 6, 2017.
@article{8546386,
  abstract     = {{Aberrant O-glycans expressed at the surface of cancer cells consist of membrane-tethered glycoproteins (T and Tn antigens) and glycolipids (Lewis a, Lewis x and Forssman antigens). All of these O-glycans have been identified as glyco-markers of interest for the diagnosis and the prognosis of cancer diseases. These epitopes are specifically detected using T/Tn-specific lectins isolated from various plants such as jacalin from Artocarpus integrifola, and fungi such as the Agaricus bisporus lectin. These lectins accommodate T/Tn antigens at the monosaccharide-binding site; residues located in the surrounding extended binding-site of the lectins often participate in the binding of more extended epitopes. Depending on the shape and size of the extended carbohydrate-binding site, their fine sugar-binding specificity towards complex O-glycans readily differs from one lectin to another, resulting in a great diversity in their sugar-recognition capacity. T/Tn-specific lectins have been extensively used for the histochemical detection of cancer cells in biopsies and for the follow up of the cancer progression and evolution. T/Tn-specific lectins also induce a caspase-dependent apoptosis in cancer cells, often associated with a more or less severe inhibition of proliferation. Moreover, they provide another potential source of molecules adapted to the building of photosensitizer-conjugates allowing a specific targeting to cancer cells, for the photodynamic treatment of tumors.}},
  articleno    = {{1232}},
  author       = {{Poiroux, Guillaume and Barre, Annick and Van Damme, Els and Benoist, Hervé and Rougé, Pierre}},
  issn         = {{1422-0067}},
  journal      = {{INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES}},
  keywords     = {{HUMAN BREAST-CANCER,RIBOSOME-INACTIVATING PROTEIN,THOMSEN-FRIEDENREICH,ANTIGEN,WHEAT-GERM-AGGLUTININ,CARBOHYDRATE-BINDING SPECIFICITIES,AMARANTHUS-LEUCOCARPUS LECTIN,MUSHROOM AGARICUS-BISPORUS,BAUHINIA-FORFICATA LECTIN,SCLEROTIUM-ROLFSII LECTIN,MOLUCCELLA-LAEVIS,LECTIN,lectin,O-glycosylation,Tn antigen,T antigen,Morniga G,peanut,lectin,cancer,diagnosis,prognosis,photodynamic therapy}},
  language     = {{eng}},
  number       = {{6}},
  pages        = {{30}},
  title        = {{Plant lectins targeting O-glycans at the cell surface as tools for cancer diagnosis, orognosis and therapy}},
  url          = {{http://doi.org/10.3390/ijms18061232}},
  volume       = {{18}},
  year         = {{2017}},
}

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