Suzanne Bohlson, Ph.D.

Bohlson, Suzanne
Director Master of Science in Biomedical Sciences
Associate Professor Microbiology and Immunology
Doctor of Osteopathic Medicine
Office Phone 515-271-1559
  • Postdoctoral Fellow, University of California Irvine, 2001- 2005
  • Ph.D. Biology, University of Notre Dame, 2001
  • M.A., Immunology, Washington University St. Louis, 1998
  • B.S. Biology, University of California Irvine, 1995

Awards and honors

2013 – NIH NIAID R56 “Characterization of a novel C1q-dependent engulfment pathway in autoimmunity”

2013 – Early Career Investigator Travel Grant, American Association of Immunologists

2009 – NIH NIAID R56 “The Regulation of Inflammation and Phagocytosis by CD93”

2007 – G. J. Thorbecke Award for excellence in host defense and inflammation research, Society for Leukocyte Biology

2006 – American Heart Association Scientist Development Grant

2006 – Arthritis Investigator Award (declined), Arthritis Foundation

2005 – Career Development Award, University of CA, Irvine

2005 – Burgess Memorial Award, University of CA, Irvine

2002 – NIH Carcinogenesis training grant postdoctoral fellowship

1996 – Lucille P. Markey pathway predoctoral fellowship

Specific cells in the body are designed to ingest dangerous particles, such as invading bacteria. These professional eating cells, or phagocytes, also eat dead or dying cells. This process of clearance of dead or dying cells is necessary to allow for the repair of damaged tissue, and to maintain normal tissue. When this process of cellular ingestion (phagocytosis) is dysregulated, the body becomes susceptible to chronic infections and autoimmunity. My laboratory focuses on phagocyte recognition and clearance events with the goal of developing therapies that strengthen the body’s ability to ingest and kill infectious particles or dead/dying cells.

Billions of cells die in the body every day by normal processes (apoptosis). These dead cells need to be recognized by phagocytes and cleared rapidly. C1q is a protein that regulates phagocytosis of dead cells. It is found in blood and expressed in response to inflammatory signals. C1q may be used by the body to modulate the response to injury and to decrease the damage associated with inflammation. We are testing C1q and related molecules called “defense collagens” for their ability to regulate these events. These studies may help develop novel therapeutics to fight inflammatory and autoimmune diseases such as atherosclerosis, rheumatoid arthritis and lupus.
Figure.  Phagocytic cells must functionally sum the signals received from the particles being detected via their diverse pattern recognition receptors to direct a gene expression program that dictates an appropriate immune response (inflammatory or anti-inflammatory). TF, transcription factor; TLR, Toll like receptor, PSR; phosphatidyl serine receptor; C1qR, C1q/MBL receptor. Artwork by Cheryl Cotman. Reproduced from Bohlson et al., 2006, Molecular Immunology (


Galvan, M. D., Hulsebus, H., Heitker, T., Zeng, E., and Bohlson, S.S.Complement protein C1q and adiponectin stimulate Mer tyrosine kinase dependent engulfment of apoptotic cells through a shared pathway. Journal of Innate Immun. 2014 Jun 17. [Epub ahead of print] PMID: 24942043

Bohlson, S.S., O’Conner, S.D., Hulsebus, H., Ho, M., and Fraser, D.A.  Complement, C1q, and C1q-related molecules regulate macrophage polarization.  Frontiers in Immunology, Aug 21, 2014.

Galvan, M.D., Foreman D.B., Zeng, E., Tan, J.C., Bohlson, S.S. Complement component C1q regulates macrophage expression of Mer tyrosine kinase to promote clearance of apoptotic cells, Journal of Immunology. 188(8):3716-23. Apr 15, 2012

Galvan MD, Greenlee-Wacker MC, and Bohlson, S.S. C1q and phagocytosis: the perfect complement to a good meal. Journal of Leukocyte Biology. 92(3):489-97. Sep, 2012

Greenlee-Wacker MC, Briseño C, Galvan M, Moriel G, Velázquez P, Bohlson, S.S. Membrane-Associated CD93 Regulates Leukocyte Migration and C1q-Hemolytic Activity during Murine Peritonitis. Journal of Immunology. 2011, Sep 15;187(6):3353-61. Epub Aug 17., 2011

Greenlee-Wacker MC, Galvan MD and Bohlson, S.S. CD93: Recent Advances and Implications in Disease. Current Drug Targets. [Epub ahead of print]. Dec 29, 2011

Kozmar, A., Greenlee-Wacker, M.C., Bohlson, S.S. Macrophage response to apoptotic cells varies with the apoptotic trigger and is not altered by a deficiency in LRP expression. Journal of Innate Immunity. 2(3): 248- 259., 2010

Greenlee, M., Sullivan, S., and Bohlson, S.S. Detection and characterization of soluble CD93 released during inflammation. Inflammation Research, July 15 , 2009

Greenlee, M.C., Sullivan, S.A., and Bohlson, S.S. CD93 and Related Family Members: Their Role in Innate Immunity. Review. Current Drug Targets. (2):130-8. Feb 9, 2008

Lillis, A., Greenlee, M., Mikhailenko, I., Pizzo S., Tenner A., Strickland, D., and Bohlson, S. Murine LRP is required for phagocytosis of targets bearing LRP ligands but is not required for C1q-triggered enhancement of phagocytosis. Journal of Immunology. 181(1): 364-373. July, 2008

Fraser, D., Arora, M., Bohlson, S.S, Lozano, E., and Tenner, A.J. Generation of Inhibitory NFκB Complexes and pCREB Correlates with the Anti-inflammatory Activity of Complement Protein C1q in Human Monocytes. J Biol Chem. 282(10):7360-7. Mar 9, 2007

Bohlson, S.S., Fraser, D., Tenner, A.J. Complement Proteins C1q and MBL are Pattern Recognition Molecules that Signal Immediate and Long Term Protective Immune Functions. Review. Molecular Immunology. 44(1-3):33-43. Jan, 2007

Fraser D., Bohlson, S.S, Jasinskiene, N., Rawal, N., Palmerini, G., Ruiz, S., Rochford, R., and Tenner, A. C1q and MBL, components of the innate immune system, modulate monocyte cytokine expression. Journal of Leukocyte Biology; 80(1):107-16. Jul, 2006

Bohlson, S.S., Silva, R. Fonseca, M.I. and Tenner, A.J. CD93 is rapidly shed from the surface of human myeloid cells in response to a variety of stimuli and the soluble form is detected in human plasma. Journal of Immunology, 175: 1239-1247., 2005

Zhang, M., Bohlson, S.S., Dy, M., and Tenner, A.J. Modulated interaction of the ERM protein, moesin, with CD93. Immunology, 115:63-73., 2005

Bohlson, S.S, Zhang, M., Ortiz, C.E., and Tenner, A.J. CD93 interacts with the PDZ doman containing protein GIPC: Implications in the modulation of phagocytosis. Journal of Leukocyte Biology, 77(1):80-9., 2005

Bohlson, S.S., Strasser, J.A., Bower, J.J and Schorey J.S.: The Role of Complement in M. avium Pathogenesis: In vitro and in vivo analysis of the Host Response in the Absence of Complement Component C3. Infection and Immunity, 69 (12) 7729-35., 2001

Blystone, S.D., Slater, S.E., Williams, M.P., Crow, M.T. and Brown, E.J.: A Molecular Mechanism of Integrin Crosstalk: αvβ3 Supression of Calcium/Calmodulin-Dependent Protein Kinase II Regulates α5β1 Function. Journal of Cell Biology, 145 (4):889-897, 1999

Roach, T.I.A., Slater, S.E., White, L., Zhang, X., Majerus, P.W., Brown, E.J., and Thomas, M.L.: The Protein Tyrosine Phosphatase SHP-1 Regulates Integrin-mediated Adhesion of Macrophages. Current Biology, 8(18):1035-1038, 1998

Blystone, S.D., Williams, M.P., Slater, S.E., and Brown, E.J.: Requirement of Integrin β3 Tyrosine 747 for β3 Tyrosine Phosphorylation and Regulation of αvβ3 Avididty. Journal of Biological Chemistry, 272 (45): 28757-28761, 1997

Roach, T.I.A., Slater, S.E., Koval, M., White, L., Cahir McFarland, E., Okumura, M., Thomas, M., and Brown, E.J. CD45 Regulates Src Family Kinase Activity associated with Macrophage Integrin-mediated Adhesion. Current Biology, 7(6):408-417, 1997

Thomas, M.L., Roach, T.I.A., Slater, S.E., White, L., Okumura, M., and Brown, E.J.: The Protein Tyrosine Phosphatase, CD45, in Adhesion and Signal Transduction. Kinases and Phosphatases in Lymphocyte and Neuronal Signaling. New York: Springer-Verlag, 1997