Glyco-Typer- A method of glycan analysis of immunocaptured proteins


Technology: Researchers at the Medical University of South Carolina have created a method and system that for the first time will enable the simultaneous glycan analysis of thousands of individual proteins found in complex protein mixtures such a serum and tissue samples.


This method involves:

(1) Array Fabrication - antibodies are spotted and glycoprotein capture of the sample is localized to specific known antibodies;

(2) MALDI Preparation - the N-glycans are released in a localized manner within the well corresponding to a specific antibody and the slide is matrix coated trapping released glycans in their area of release;

(3) MALDI MSI - is performed and structural glycan information is obtained for each captured protein, spot by spot. 



This method allows for the generation of structural glycan information for hundreds or thousands of individual glycoprotein targets in an array format.  As shown in the image below, specific glycan profiles will be generated for each target protein within the array, providing precise and highly detailed information on protein glycosylation across a diverse sample with high specificity to each antibody target.  This will provide researchers and clinicians with the means to observe any potential biomarker that is either glycoprotein or a protein itself, which represent nearly all currently utilized biomarkers for cancer.  Further, with this method it will become possible to observe the changes in the N-linked glycosylation of cells surface and secreted proteins that are known to occur in many cancers. 



Overview: Alterations in glycosylation of glycoproteins and extracellular matrix molecules have long been associated with the development and progression of many types of cancer and other diseases.  With N-linked glycosylation being particularly associated with cancer development and progression.  Under the current state of the art, evaluating these changes experimentally involves glycan analysis of complex protein mixtures or the analysis of a few specific individual glycoproteins.  The most common approach is to perform glycan analysis on pools of released glycans without any connection to the protein carrier.  When analysis is done on the protein carrier, this generally requires large amounts of protein and is done one at a time.  Thus, current methods require a tradeoff where you can either have glycan information for a few proteins analyzed one by one with site of glycan attachment, or data for groups of proteins or glycans (but not both together).


Given the limitations and arduous nature of glycan analysis utilizing the current standardized methods, the full potential of glycan analysis in disease diagnosis and treatment has not been realized.  Further, current methods to specifically determine the glycans on specific proteins in complex mixtures are lacking.  From a biomarker perspective this is important as many changes in glycosylation have been observed in cancer and are actively being developed as biomarkers. The biomarker potential of the glycans attached to single protein have shown great promise.  The biomarker potential of the glycans on hundreds of proteins analyzed simultaneously is tremendous.  This invention provides the opportunity for a whole new platform for biomarker discovery and validation, creating a new method to interrogate the role of N-linked glycans in cancer development, diagnosis and treatment.


Applications: glycan analysis, glycoproteomics, cancer diagnosis, cancer treatment, biomarker identification and discovery, target validation.



Broad Spectrum Analysis:  Provides the ability to analyze hundreds or thousands of glycoproteins simultaneously

High Specificity:  Glycosylation data for each target protein is highly specific.

Ease of Use:  A simple method that requires a relatively small sample size.


Key Words: glycan, glycoprotein, glycosylation, cancer, biomarker


Inventors: Anand Mehta, Richard Drake, Brian Haab, Peggi Angel

Patent Status: PCT Application PCT/US2019/35133 filed June 3, 2019       

MUSC-FRD Technology ID: P1884

Licensing Status: Available for licensing



Patent Information:
For Information, Contact:
Troy Huth
Assoc Director
MUSC Foundation for Research Development
Anand Mehta
Richard Drake
Brian Haab
Peggi Angel
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