Jean-Philippe Julien

Jean-Philippe Julien

Assistant Professor

BSc, McGill University, 2005, as a Loran Scholar
PhD, University of Toronto, 2010
Postdoc, The Scripps Research Institute, 2010-2014

Address Peter Gilgan Centre for Research and Learning (PGCRL), Room 20-9703
686 Bay St.
Toronto, ON M5G 0A4
Lab Julien laboratory
Lab Phone 416-813-7654, ext. 309425
Office Phone 416-813-7654, ext. 309424
Email jean-philippe.julien@sickkids.ca

My laboratory is interested in the structure/function study of the B cell receptor and co-receptors.

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Research Lab

Dr. Julien’s laboratory at The Hospital for Sick Children Research Institute characterizes B cell glycoprotein receptors by using a combination of biochemical, biophysical, immunological and structural techniques. We are always looking for driven and enthusiastic scientists with the passion to apply his/her knowledge and creativity towards the structure/function study of biologically-important targets.

Don’t hesitate to contact us if you’re interested in becoming part of our team!

Learn more: Julien laboratory

Research Description

Targeting B cell receptors in vaccine and disease

Dr. Julien is interested in the structure/function study of the B cell receptor and its co-receptors. In addition to the B cell receptor (BCR), which is the precursor of the secreted antibody, the B cell possesses several unique surface molecules that are involved in regulating B cell development and function, communicating with the extracellular environment, and interpreting the BCR signal. These critical molecules have mostly remained structurally uncharacterized.

Of particular interest, Dr. Julien focuses on the characterization of the BCR, and co-receptors using integrated structural and biophysical techniques. Whereas some co-receptors enhance Ca2+ responses by lowering the threshold of BCR signals, others controls follicular B cell survival and negatively regulates signaling. Careful modulation of these BCR co-receptors can therefore lead to extremely effective adjuvant strategies.

A better understanding of the structure and function of these cell surface molecules, as well as those that propagate intracellular signals will not only impact our ability to design more effective vaccines, but also provide unique sites to specifically target deregulated B cells in acute lymphoblastic leukemia (B-ALL) and in autoimmune diseases, such as Rheumatoid Arthritis (RA) and Systemic lupus erythematosus (SLE).

Publications

View all publications on PubMed

Crystal structure of a soluble cleaved HIV-1 envelope trimer.
Julien JP, Cupo A, Sok D, Stanfield RL, Lyumkis D, Deller MC, Klasse PJ, Burton DR, Sanders RW, Moore JP, Ward AB, Wilson IA.
Science. 2013. 342(6165):1477-83.  Read

Cryo-EM structure of a fully glycosylated soluble cleaved HIV-1 envelope trimer.
Lyumkis D, Julien JP, de Val N, Cupo A, Potter CS, Klasse PJ, Burton DR, Sanders RW, Moore JP, Carragher B, Wilson IA, Ward AB.
Science. 2013. 342(6165):1484-90.  Read

Rational HIV immunogen design to target specific germline B cell receptors.
Jardine J*, Julien JP*, Menis S*, Ota T, Kalyuzhniy O, McGuire A, Sok D, Huang PS, MacPherson S, Jones M, Nieusma T, Mathison J, Baker D, Ward AB, Burton DR, Stamatatos L, Nemazee D, Wilson IA, Schief WR.
Science. 2013. 340(6133):711-6.  Read

Asymmetric recognition of the HIV-1 trimer by broadly neutralizing antibody PG9.
Julien JP*, Lee JH*, Cupo A, Murin CD, Derking R, Hoffenberg S, Caulfiled MC, King CR, Marozsan AJ, Klasse PJ, Sanders RW, Moore JP, Wilson IA, Ward AB.
Proc Natl Acad Sci U.S.A. 2013. 110(11):4351-6.  Read