Over 9500 phosphorylation sites tracked in human cells for regulation by
a major bacterial pathogen for human disease
VANCOUVER, Sept. 23, 2011 /PRNewswire/ - British Columbia - Kinexus
Bioinformatics Corporation, a world-leader in molecular intelligence
research, announced the publication this week in the journal Science
the results of a major study to investigate the host signalling
pathways that are impacted by Salmonella enterica, a food-borne bacteria that is a leading cause of food poisoning in
North America and around the world. The study was undertaken in
collaboration with researchers at the Centre for High Throughput
Biology at the University of British Columbia (UBC). Mass spectrometric
analyses revealed that more than 24% of 9500 phosphorylation sites
tracked in human cells were significantly altered with 20 minutes of
Salmonella infection. Phosphosites often function as on/off switches to
regulate intracellular communication systems and their phosphorylation
is catalyzed by protein kinases. Application of Kinexus' Kinase
Predictor algorithm for 493 human protein kinases against each of the
top Salmonella affected phosphosites permitted identification of
specific protein kinases that are affected by Salmonella, including the
proto-oncogene-encoded protein kinase Pim1. Specific inhibition of Pim1
in follow up studies was found to mitigate some of the pathogen effects
of this bacteria, and implicated this kinase as a possible target for
therapeutic drug intervention.
Over 100,000 human phosphosites in over 14,000 of the 23,000 proteins
encoded by the human genome have now been experimentally confirmed.
This study has led to the identification of over 6000 previously
unknown phosphosites, and these have been posted for open access on the
Kinexus PhosphoNET website (http://www.phosphonet.ca). Kinexus'
bioinformatics programs have led to the prediction and characterization
of over 650,000 human phosphosites.
"The mass spectrometry analyses were performed at the Centre for High
Throughput Biology at UBC, and the work represents one of the major
studies of this kind undertaken to date" commented Dr. Steven Pelech,
President and Chief Scientific Officer of Kinexus and a professor in
the Department of Medicine at the University of British Columbia. "In
combination with the predictive algorithms developed at Kinexus, it is
becoming possible to map out the complex architecture of cell
signalling networks and identify the sites of action of toxins that are
produced by pathogenic viruses and bacteria."
For 12 years, Kinexus has been a unique provider of proteomics services
to academic and industrial laboratories to track protein kinases and
their phosphoprotein targets in experimental tissue and cell specimens.
The company has developed a diverse panel of microarrays and
complementary technologies that can monitor the presence and activity
levels of hundreds of kinases and their targets, their interactions,
and the effects of promising drug candidates. The application of this
knowledge positions Kinexus and its clients for improved disease
diagnosis and personalized drug therapies to improve human health.
SOURCE Kinexus Bioinformatics Corporation