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, antibodies, 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 signalling. Careful modulation of these BCR co-receptors can lead to extremely effective adjuvant strategies towards the development of vaccines against malaria and HIV.

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).

Awards & Distinctions

2017 — Canada Research Chair in Structural Immunology

Courses Taught

BCH 2024H Engineering vaccines: development to deployment
BCH473Y Advanced Research Project in Biochemistry

Publications

View all publications on PubMed

Molecular definition of multiple sites of antibody inhibition of malaria transmission-blocking vaccine antigen Pfs25.
Scally SW, McLeod B, Bosch A, Miura K, Liang Q, Carroll S, Reponen S, Nguyen N, Giladi E, Rämisch S, Yusibov V, Bradley A, Lemiale F, Schief WR, Emerling D, Kellam P, King CR, Julien JP.
Nat Commun. 2017 Nov 16; 8:1568. doi: 10.1038/s41467-017-01924-3.  Read

Rare PfCSP C-terminal antibodies induced by live sporozoite vaccination are ineffective against malaria infection.
Scally SW*, Murugan R*, Bosch A, Triller G, Costa G, Mordmüller B, Kremsner PG, Sim BKL, Hoffman SL, Levashina EA, Wardemann H#, Julien JP#.
J Exp Med. 2017 Nov 22. doi: 10.1084/jem.20170869.  Read

Molecular basis of human CD22 function and therapeutic targeting.
Ereño-Orbea J*, Sicard T*, Cui H, Mazhab-Jafari MT, Benlekbir S, Guarné A, Rubinstein JL, Julien JP.
Nat Commun. 2017 Oct 2; 8:764. doi: 10.1038/s41467-017-00836-6.  Read

Natural Parasite Exposure Induces Protective Human Anti-Malarial Antibodies.
Triller G*, Scally SW*, Costa G, Pissarev M, Kreschel C, Bosch A, Marois E, Sack BK, Murugan R, Salman AM, Janse CJ, Khan SM, Kappe SHI, Adegnika AA, Mordmüller B, Levashina EA, Julien JP#, Wardemann H#.
Immunity. 2017 Dec 19; 47: 1–13. doi: 10.1016/j.immuni.2017.11.007.  Read

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. doi: 10.1126/science.1245625.  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. doi: 10.1126/science.1245627.  Read