Please use this identifier to cite or link to this item: https://ahro.austin.org.au/austinjspui/handle/1/16442
Title: Antibody recognition of aberrant glycosylation on the surface of cancer cells
Austin Authors: Soliman, Caroline;Yuriev, Elizabeth;Ramsland, Paul A 
Affiliation: School of Science, RMIT University, Bundoora, Victoria, Australia
Medicinal Chemistry, Monash Institute of Pharmaceutical Sciences, Monash University, Parkville, Victoria, Australia
Department of Immunology, Monash University, Alfred Medical Research and Education Precinct, Melbourne, Victoria, Australia
Department of Surgery, Austin Health, The University of Melbourne, Heidelberg, Victoria, Australia
Centre for Biomedical Research, Burnet Institute, Melbourne, Victoria, Australia
Issue Date: Jun-2017
metadata.dc.date: 2016-11-04
Publication information: Current Opinion in Structural Biology 2017; 44: 1-8
Abstract: Carbohydrate-binding antibodies and carbohydrate-based vaccines are being actively pursued as targeted immunotherapies for a broad range of cancers. Recognition of tumor-associated carbohydrates (glycans) by antibodies is predominantly towards terminal epitopes on glycoproteins and glycolipids on the surface of cancer cells. Crystallography along with complementary experimental and computational methods have been extensively used to dissect antibody recognition of glycan epitopes commonly found in cancer. We provide an overview of the structural biology of antibody recognition of tumor-associated glycans and propose potential rearrangements of these targets in the membrane that could dictate the complex biological activities of these antibodies against cancer cells.
URI: http://ahro.austin.org.au/austinjspui/handle/1/16442
DOI: 10.1016/j.sbi.2016.10.009
PubMed URL: https://pubmed.ncbi.nlm.nih.gov/27821276
Type: Journal Article
Appears in Collections:Journal articles

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