Antibody recognition of aberrant glycosylation on the surface of cancer cells.
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.
School of Science, RMIT University, Bundoora, Victoria 3083, Australia.
Caroline
C
Soliman
Medicinal Chemistry, Monash Institute of Pharmaceutical Sciences, Monash University, Parkville, Victoria 3052, Australia. Electronic address: elizabeth.yuriev@monash.edu.
Elizabeth
E
Yuriev
School of Science, RMIT University, Bundoora, Victoria 3083, Australia; Department of Immunology, Monash University, Alfred Medical Research and Education Precinct, Melbourne, Victoria 3004, Australia; Department of Surgery Austin Health, University of Melbourne, Heidelberg, Victoria 3084, Australia; Centre for Biomedical Research, Burnet Institute, Melbourne, Victoria 3004, Australia. Electronic address: paul.ramsland@rmit.edu.au.
Paul A
PA
Ramsland
D000595:Amino Acid Sequence; D000818:Animals; D000906:Antibodies / Q000737:chemistry / Q000276:immunology*; D000939:Epitopes / Q000276:immunology; D006031:Glycosylation; D006801:Humans; D009369:Neoplasms / Q000276:immunology* / Q000378:metabolism / Q000473:pathology*; D011134:Polysaccharides / Q000276:immunology / Q000378:metabolism
D000906:Antibodies; D000939:Epitopes; D011134:Polysaccharides