Mass Spectrometry Investigation of Glycosylation Aberration via De-N-Glycopeptide Analysis
Vivekananda Shetty A B C and Ramila Philip A
+ Author Affiliations
- Author Affiliations
A Immunotope, Inc., 3805 Old Easton Road, Doylestown, PA 18902, USA.
B Current address: Progenics Pharmaceuticals, Inc., 777 Old Saw Mill River Road, Tarrytown, NY 10591, USA.
C Corresponding author. Email: vivek@immunotope.com
Dr Vivek Shetty received his Ph.D in mass spectrometry from the Indian Institute of Chemical Technology, India. He was also the recipient of the prestigious Humboldt Fellowship. Dr Shetty has published 42 research articles on mass spectrometry-based genomics and proteomics. As a Director at Immunotope, Inc., he led the analytical team which discovered novel glycoprotein biomarkers and MHC peptide antigens in cancer and infectious diseases. He is currently working as a scientist at Progenics Pharmaceuticals, Inc., in New York. Dr Shetty's research interests are in glycoprotein biomarker and MHC peptide antigen discovery, cysteine proteomics, and the characterization of antibodies and antibody drug conjugates. |
Dr Ramila Philip is the scientific founder of Immunotope, Inc., and is currently the President and Chief Scientific Officer. She earned her Ph.D. in immunology in India and did post-doctoral training at the Institute of Immunology, Basel, Switzerland, and was a junior faculty member at the Cancer Research Institute, UCSF. She has held a number of senior level positions in pharmaceutical and biotechnology companies, and currently holds an adjunct professorship at Drexel University and a professorship at the Institute for Hepatitis and Virus Research. Dr Philip's research focus is in immunotherapy and clinical studies. She has over 75 peer-reviewed publications to her name. |
Australian Journal of Chemistry 66(7) 770-780 https://doi.org/10.1071/CH13159
Submitted: 9 April 2013 Accepted: 7 June 2013 Published: 10 July 2013
Abstract
Proteomics research on glycan alterations has received great attention owing to their implications in disease initiation and progression. Determination of the glycoprotein expression remains one of the most challenging tasks as the glycan residues in a given glycoprotein exist in complex branched structures and differ in linkage. In view of the vital role of glycan changes in cellular processes and disease progression, there has been an increased interest in developing methodologies for the detection of these changes. A subset of proteomics methods are discussed here that demonstrate the utility of the glycan-free de-N-glycopeptide analysis for the screening of complex glycoproteome as well as discovery of glycopeptide/glycoprotein biomarkers.
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