Glycoprotein targeting and other applications of lectins in biotechnology

• Published in: Current protein & peptide science Vol. 8; no. 3; p. 261
• Main Authors: Naeem, Aabgeena, Saleemuddin, M, Khan, Rizwan Hasan
• Format: Journal Article
• Language: English
• Published: United Arab Emirates 01-06-2007
• Subjects: Biotechnology - methods; Carbohydrates - chemistry; Cell Membrane - chemistry; Glycoproteins - chemistry; Humans; Killer Cells, Natural - drug effects; Plant Lectins - chemistry; Plant Lectins - toxicity; Plant Proteins - chemistry; T-Lymphocytes - drug effects; Tumor Cells, Cultured - drug effects
• ISSN: 1389-2037
• DOI: 10.2174/138920307780831811

Glycoconjugates comprise a variety of structures, include glycoproteins and glycolipids and are found on the surfaces of animal and plant cells, as well as on the surface of microorganisms. Determination of the structure and the distribution of glycoconjugates on cell surfaces are important for the understanding their biological function. Lectins are useful to investigate protein-carbohydrate interactions, because they have specificity for defined carbohydrate structure. They have been implicated in cell-to-cell recognition and signaling, blood group typing, in immune recognition process, and various other biological processes, such as viral, bacterial, mycoplasmal and parasitic infections, fertilization, cancer metastasis, growth and differentiation. Once thought to be confined to plant seeds, lectins are now recognized as ubiquitous in virtually all living systems, ranging from viruses and bacteria to animals. Plant lectins provide a rich source of carbohydrate-recognizing protein reagents for glycobiologists and biotechnologists. Biotechnology offers the therapeutic use of lectin against certain life threatening diseases such as human immunodeficiency virus and cancer. This review presents a comprehensive summary of research efforts that focus on the actual and potential uses and advantages of using lectins to target glycoproteins and also glycoproteins to target lectins.