Editorials

 

- Third International Conference of the Canadian Proteomics Initiative -
May 23rd to 27th, 2003 - University of British Columbia, Vancouver, BC
by Chris Dambrowitz, Genome Prairie (dambro@genomeprairie.ca)

This meeting was sponsored by PENCE (the Canadian Protein Engineering National Centre of Excellence), Genome BC, and several other Canadian research organizations.  A dominant subtext of the event involved the future of proteomics research in Canada - and what initiatives might be responsible for shaping that future.  This report seeks to provide a view of the themes and undercurrents of the conference, rather than an all-inclusive review of the scientific presentations.  For readers interested in the latter, the abstracts posted at http://www.cpi03.org provide such a reference.

In her opening address, Martha Piper, President of the University of British Columbia (UBC), announced that UBC would be adding ten new faculty positions in proteomics and bioinformatics.  These researchers will be part of the Biotechnology Laboratory, based in the 7,400-square metre Michael Smith Building currently under construction and slated for completion in late 2004.

The first scientific presentations were by researchers from Seattle’s Institute for Systems Biology.  Ruedi Aebersold discussed novel applications of ICAT technology for quantitative proteome analysis - particularly focusing on comparative and quantitative analysis of protein complexes.  John Aitchison provided an overview of the complexity and data-richness involved in a systems-biology approach to understanding the dynamics of a single organelle, the peroxisome.  Both of these ISB-based presenters have strong research roots and current collaborations in Canada. Not only did the scope and success of their presented research set the bar for subsequent speakers at this meeting, but also highlighted the challenge before Canadian proteomics researchers as the future is contemplated.  Proteomics research on a grand scale is demonstrably feasible in Canada - do we also have the scientific vision, operational clarity, and political will to capitalize on that potential?

Day 2 of CPI ’03 began with Fiona Brinkman’s (Simon Fraser University) description of the BAE-watch database for potentially identifying patterns in the evolution of microbial virulence - and an outline of strategies for microbial control derived from Sun Tzu’s Art of War.  Mitsu Ikura’s (University of Toronto) discussion of calcium-induced conformational changes in calmodulin and related protein domains highlighted the perspective that large-scale proteomic methods may still require support from targeted studies on each individual protein class, in a manner that may not be amenable to high-throughput techniques.  The tension between the classical protein biochemistry “one-protein-one lab-one lifetime” approach, and the massively-parallel paradigm of proteomics again became a predominant theme of the day, as echoed through presentations, audience questions, and coffee-break discussions.

Presentations that focused on structural proteomics followed, by Natalie Strynadka (UBC) regarding high-throughput structural studies of membrane proteins by X-ray crystallography, and by Lewis Kay (U of T) on multi-dimensional NMR analysis of high-MW proteins and multi-protein complexes.  The first of these two talks particularly emphasized that the answer to a case-by-case approach to resolving protein structures lies in the judicious selection of experimental algorithms for batch processing that permit high-throughput structural analysis. 

McGill’s John Bergeron presented a view of single-organelle proteomic analysis efforts by LC/MS/MS, with emphasis on the study of the endoplasmic reticulum.  A practical note, highlighting the bottleneck presented by available bioinformatic techniques, was his estimate that 5% of lab time is spent actually performing wet-lab work (such as organelle isolation, sample prep, etc.), while the other 95% is dedicated to matching his group’s MS/MS data to protein databases.  Tony Pawson (SLRI/U of T), in his discussion of approaches to assembling multiprotein regulatory complexes from analysis of protein domain interactions, drew chuckles by commenting that his emphasis might be described as “one-DOMAIN-one-lab-one-lifetime”.  Bob Olafson described the evolution of the UVictoria-Genome BC Proteomics Centre from a protein-chemistry core facility in the early ‘80s to its present incarnation as a high-throughput facility providing LC/MS/MS and ICAT services (among others) to academic, industrial and governmental research groups.  During the Q&A period, vigorous discussion focused on the accessibility of such services to Canadian academic groups, and also on the problem of obtaining support for large-scale “discovery science” proposals within the confines of the traditional Canadian research funding paradigm. 

 

On the heels of this discussion, U of Toronto’s Andrew Emili brought into the open key issues that had been hinted at for much of the conference.  In presenting his group’s approach to large-scale analysis of proteome dynamics during myoblast differentiation, Emili’s key theme was that algorithms, not MS methodologies, identify proteins. Automation and ultrahigh throughput techniques are absolutely essential to the success of discovery-science projects.  In a succinct summary of one of the meeting’s key undercurrents (and a contentious one, based on the resultant rise in tension in the room), Emili asserted that what proteomics research is really all about is “Go Big, or Go Home”.  Proteometricians should leave (traditional) biology to the biologists - and should instead focus on proteomics, providing a holistic view of biology at the systems level.  The challenges that this paradigm shift presents to the Canadian research community, and the divisions within that community on this issue, were evident at this meeting.

One of the most anticipated sessions of CPI ’03 was a forum on the Shape of Proteomics in Canada.  The session’s organizing committee had selected several speakers to provide context for discussion.  David Griller gave an excellent presentation of SECOR survey results indicating that Canadian proteomics must support bold initiatives having strong socioeconomic impact, and maintain a global orientation in commercialization in order to capture economic benefits for Canada.  Subsequent presenters, including Aled Edwards (U of T), John Bergeron (under the HUPO banner), Francis Ouellette (UBC), Michel Chretien (U Ottawa), Roger Foxall (Genome BC), Steve Armstrong (Genome Atlantic), and Peter Freeman (ANPI), described various regional or strategic initiatives relating to proteomics-related networks.  Finally, a plan for a Canadian Proteomics Network was outlined that might contribute to a national infrastructure for research in proteomics and protein engineering.  A steering committee, potentially composed of PENCE’s Steve Withers, Joel Weiner, Peter Lewis, John Bergeron and the NRC’s Bob Boyd, would take responsibility for determining the mandate, objectives, strategy and budget of such a national network.  Unfortunately, time constraints prevented an assessment of grassroots response to the outlined initiative, leaving issues raised through this session open for future discussion.

The final day of speaker presentations (leaving two days for tutorial sessions on various topics) was similar in tone to the first - several excellent talks that highlight the scope attainable through proteomic studies.  Mike Moran of MDS Proteomics reviewed MDS.P’s technology for measuring changes in protein expression, organellar proteome, protein-protein interactions, and phospho-protein profiles in response to disease and to drug treatments, including MDS.P’s new software and hybrid FT-ICR mass spectrometry instrumentation. NIST’s John Moult reviewed his group’s study of the relationship between mild destabilizing effects on canonical protein structures caused by single nucleotide variations and disease, shedding light on the system-engineering processes that underlie the robustness of protein networks.  Finally, Chris Dobson (Cambridge University) demonstrated the effective combination of experimental data and simulations to identify surface features related to protein folding and mis-folding, and the relationship between protein folding, self-assembly, and structural evolution.  (Unfortunately, this reviewer missed the opportunity to attend the latter two talks, and so is relying on secondhand information for their description.)

The next Canadian Proteomics Initiative Conference is currently slated for May 2004, in Montreal QC.


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