High throughput tools to profile the glycome of protists

CARB 90

Daniel M. Ratner, dratner@bu.edu1, Sulagna Banerjee2, Anirban Chatterjee2, Phillips W. Robbins2, and John Samuelson2. (1) Molecular and Cell Biology, Boston Medical Center, 715 Albany St., Evans 4, Rm438, Boston, MA 02118, (2) Molecular and Cell Biology, Boston Univeristy Goldman School of Dental Medicine, 715 Albany St., Evans 4, Rm438, Boston, MA 02118
Progress in the field of glycomics has been hindered by the need for new biophysical tools to study glycans and glycoconjugates. Lacking a biological amplification counterpart to the polymerase chain reaction (PCR) or recombinant protein expression, glycobiologists often are forced to make the most of small quantities of isolated material. To address this need for new and more sensitive tools for glycobiology, tandem mass spectrometry has been employed for the characterization of protein glycosylation in protists. Described is an effort to map N-glycan occupancy among the secreted proteins of Giardia lamblia. Utilizing glycan-specific lectin affinity, Giardia glycoproteins were enriched from the secretome and subjected to LC/MS/MS analysis. SEQUEST (University of Washington) data processing was successfully used to search the isolated proteins for carbohydrate modifications. In addition to N-linked glycosylation, this MS-based method is also amendable to the study of O- and O-phosphodiester-linked glycans.
 

General Papers: Analytical Chemistry and Biochemistry of Carbohydrates and Derivatives
8:30 AM-12:30 PM, Thursday, 30 March 2006 Georgia World Congress Center -- B409, Oral

Division of Carbohydrate Chemistry

The 231st ACS National Meeting, Atlanta, GA, March 26-30, 2006