European Peptide Society

Free interactive webinar:
Challenges and Solutions for In-Depth Coverage
and Quantitation of the Immunopeptidome

Overview

The cellular immune response depends upon T cell recognition of peptides presented on the surface of cells. Tens to hundreds of thousand different MHC-bound surface peptides (the immunopeptidome) are simultaneously displayed for scrutiny by T cells.

Although mass spectrometry offers a powerful approach for measurement of antigen, the informatics required for MHC peptides is one of the most extreme challenges faced in any area of study in proteomics...

The webinar covers:

• Data is shown from the new TripleTOF^TM 5600 mass spectrometry system that combines high speed with high resolution to deliver greater numbers of high-confidence peptide identifications and quantitative measurements on these complex samples than ever before.
  
• The Paragon^TM Algorithm in ProteinPilot^TM Software that is uniquely able to handle the 'no enzyme' search challenge of this extreme identification analysis regime is also discussed.
  
• In addition, complementary results from targeted mass spectral techniques to more readily identify pathogen or antigen specific peptides are shown for application in studies of immunisation, infection and disease.

More Information...

The cellular immune response depends upon T cell recognition of peptides presented on the surface of cells. These peptides are derived from the degradation of proteins from either intracellular or extracellular sources and are presented on the cell surface by molecules encoded by the Major Histocompatibility Complex (MHC).

Tens to hundreds of thousand different MHC-bound peptides (the immunopeptidome) are simultaneously displayed for scrutiny by T cells. The intracellular processing, location and the amount of a specific peptide antigen that is displayed to T cells impacts dramatically on the effectiveness of the ensuing immune response.

Mass spectrometry offers a powerful approach to the measurement of antigen present in vitro and in vivo, but the identification informatics analysis required for the study of MHC peptides is one of the most extreme challenges faced in any area of study in proteomics because these endogenous peptides lack a predictable digestion pattern.

Prof. Anthony Purcell Department of Biochemistry & Molecular Biology University of Melbourne, Australia Prof. Purcell biography >>>	Dr. Sean Seymour Senior Staff Scientist AB SCIEX Dr. Seymour biography >>>
Prof. Purcell: Biography Associate Professor Anthony W. Purcell is a senior research fellow in the Department of Biochemistry and Molecular Biology and a laboratory head at the Bio21 Molecular Science and Biotechnology Institute at the University of Melbourne. His research interests include mass spectrometry, proteomics and the biochemical definition of peptides recognised by the immune system, with a particular emphasis on the role of post-translationally modified antigens and their role in health and disease. Dr Purcell also leads a peptide based vaccine program that aims to design highly specific and stable peptide like lead compounds for inclusion in anti-tumor immunotherapies. In 2008, Dr Purcell was awarded a NH&MRC Senior Research Fellowship and the Roche Medal from the Australian Society for Biochemistry and Molecular Biology. He was the recipient of the Allan Stephens Ward from Arthritis Australia and a Grimwade Research Fellowship in 2005.	Dr. Seymour: Biography Sean Seymour received his Ph.D. in chemistry from the University of California, Berkeley where he trained with Professor Judith P. Klinman, exploring the role of protein dynamics and quantum mechanical tunneling in enzymatic catalysis using kinetics and biophysical techniques. This protein chemistry background and data analysis experience served as the foundation for a transition from the laboratory to bioinformatics. He is now a senior staff scientist entering his 10th year at AB SCIEX and its predecessor companies where he has focused on proteomics informatics and mass spectrometry application development. As the architect of the ProteinPilotTM software product, his research has focused on methodology development for better protein identification and quantitation through the development of the ParagonTM and Pro GroupTM algorithms and related methods. He has been actively involved in numerous community efforts in proteomics, including the HUPO Proteomics Standards Initiative (PSI), MCP Guidelines development, and the ABRF Proteome Informatics Research Group (iPRG), where he served as the founding chair.