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Overview of the structure-function relationships of mannose-specific lectins from plants, algae and fungi

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Abstract
To date, a number of mannose-binding lectins have been isolated and characterized from plants and fungi. These proteins are composed of different structural scaffold structures which harbor a single or multiple carbohydrate-binding sites involved in the specific recognition of mannose-containing glycans. Generally, the mannose-binding site consists of a small, central, carbohydrate-binding pocket responsible for the "broad sugar-binding specificity" toward a single mannose molecule, surrounded by a more extended binding area responsible for the specific recognition of larger mannose-containing N-glycan chains. Accordingly, the mannose-binding specificity of the so-called mannose-binding lectins towards complex mannose-containing N-glycans depends largely on the topography of their mannose-binding site(s). This structure-function relationship introduces a high degree of specificity in the apparently homogeneous group of mannose-binding lectins, with respect to the specific recognition of high-mannose and complex N-glycans. Because of the high specificity towards mannose these lectins are valuable tools for deciphering and characterizing the complex mannose-containing glycans that decorate both normal and transformed cells, e.g., the altered high-mannose N-glycans that often occur at the surface of various cancer cells.
Keywords
HUMAN-IMMUNODEFICIENCY-VIRUS, AMINO-ACID-SEQUENCE, CARBOHYDRATE-BINDING, AGENTS, ANTI-HIV ACTIVITY, ENVELOPE GLYCOPROTEIN GP120, JACALIN-RELATED, LECTINS, MANNOSE/GLUCOSE-SPECIFIC LECTIN, CANAVALIA-BRASILIENSIS LECTIN, PINELLIA-TERNATA AGGLUTININ, GLYCAN-SPECIFIC LECTIN, lectin, plant, fungi, mannose-binding specificity, structure, function, use as tools

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MLA
Barre, Annick, et al. “Overview of the Structure-Function Relationships of Mannose-Specific Lectins from Plants, Algae and Fungi.” INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, vol. 20, no. 2, 2019, doi:10.3390/ijms20020254.
APA
Barre, A., Bourne, Y., Van Damme, E., & Rouge, P. (2019). Overview of the structure-function relationships of mannose-specific lectins from plants, algae and fungi. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 20(2). https://doi.org/10.3390/ijms20020254
Chicago author-date
Barre, Annick, Yves Bourne, Els Van Damme, and Pierre Rouge. 2019. “Overview of the Structure-Function Relationships of Mannose-Specific Lectins from Plants, Algae and Fungi.” INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES 20 (2). https://doi.org/10.3390/ijms20020254.
Chicago author-date (all authors)
Barre, Annick, Yves Bourne, Els Van Damme, and Pierre Rouge. 2019. “Overview of the Structure-Function Relationships of Mannose-Specific Lectins from Plants, Algae and Fungi.” INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES 20 (2). doi:10.3390/ijms20020254.
Vancouver
1.
Barre A, Bourne Y, Van Damme E, Rouge P. Overview of the structure-function relationships of mannose-specific lectins from plants, algae and fungi. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES. 2019;20(2).
IEEE
[1]
A. Barre, Y. Bourne, E. Van Damme, and P. Rouge, “Overview of the structure-function relationships of mannose-specific lectins from plants, algae and fungi,” INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, vol. 20, no. 2, 2019.
@article{8665358,
  abstract     = {To date, a number of mannose-binding lectins have been isolated and characterized from plants and fungi. These proteins are composed of different structural scaffold structures which harbor a single or multiple carbohydrate-binding sites involved in the specific recognition of mannose-containing glycans. Generally, the mannose-binding site consists of a small, central, carbohydrate-binding pocket responsible for the "broad sugar-binding specificity" toward a single mannose molecule, surrounded by a more extended binding area responsible for the specific recognition of larger mannose-containing N-glycan chains. Accordingly, the mannose-binding specificity of the so-called mannose-binding lectins towards complex mannose-containing N-glycans depends largely on the topography of their mannose-binding site(s). This structure-function relationship introduces a high degree of specificity in the apparently homogeneous group of mannose-binding lectins, with respect to the specific recognition of high-mannose and complex N-glycans. Because of the high specificity towards mannose these lectins are valuable tools for deciphering and characterizing the complex mannose-containing glycans that decorate both normal and transformed cells, e.g., the altered high-mannose N-glycans that often occur at the surface of various cancer cells.},
  articleno    = {254},
  author       = {Barre, Annick and Bourne, Yves and Van Damme, Els and Rouge, Pierre},
  issn         = {1422-0067},
  journal      = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
  keywords     = {HUMAN-IMMUNODEFICIENCY-VIRUS,AMINO-ACID-SEQUENCE,CARBOHYDRATE-BINDING,AGENTS,ANTI-HIV ACTIVITY,ENVELOPE GLYCOPROTEIN GP120,JACALIN-RELATED,LECTINS,MANNOSE/GLUCOSE-SPECIFIC LECTIN,CANAVALIA-BRASILIENSIS LECTIN,PINELLIA-TERNATA AGGLUTININ,GLYCAN-SPECIFIC LECTIN,lectin,plant,fungi,mannose-binding specificity,structure,function,use as tools},
  language     = {eng},
  number       = {2},
  pages        = {49},
  title        = {Overview of the structure-function relationships of mannose-specific lectins from plants, algae and fungi},
  url          = {http://dx.doi.org/10.3390/ijms20020254},
  volume       = {20},
  year         = {2019},
}

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