Edward Campbell, PhD

Edward Campbell, PhD


Ph.D. University of Illinois at Chicago

Major Research Interests: Cellular factors promoting or inhibiting HIV-1 infection; prion-like spread of amyloid proteins in neurodegenerative diseases; the role of inflammation in disease pathogenesis. 

My lab is focused on using imaging-based approaches to understand the cellular mechanisms of disease pathogenesis. By understanding the mechanistic basis of disease in cells, we hope to uncover opportunities to develop therapeutic strategies to improve the lives of patients living with currently incurable diseases.

We are interested in understanding the interactions occurring between HIV-1 and target cells that lead to, or prevent, productive infection. This includes understanding how cellular proteins, termed restriction factors, can inhibit HIV-1 infection, and how HIV-1 and other retroviruses can evade these restriction factors to replicate efficiently. We are also working to understand how HIV-1 interacts with cellular proteins to facilitate infection, specifically examining how HIV-1 engages the microtubule cytoskeleton and nuclear pore complex during infection.

We are also interested in understanding the “virus like” transmission of amyloid proteins that occur in neurodegenerative diseases. By understanding the mechanism by which these proteins, such as alpha-synuclein in Parkinson’s disease, spread from cell to cell, we hope to identify opportunities to arrest disease development in patients with Parkinson’s disease, Alzheimer’s disease and Huntington’s disease. We are currently examining how these amyloid proteins enter neurons and induce cellular dysfunction that ultimately drives the continued spread of these amyloid proteins and their associated pathology.

Finally, we are interested in understanding how inflammation drives the pathogenesis of numerous human diseases. To this end, we have developed a novel biosensor which can monitor inflammation in mouse models of human disease. The ability to monitor inflammation in living animals may provide experimental tools with which to better understand and treat numerous human diseases.

Adarsh Dharan, Silvana Opp, Omar Abdel-Rahim , Sevnur Komurlu Keceli, Sabrina Imam, Felipe Diaz-Griffero, Edward M. Campbell. Bicaudal D2 facilitates the cytoplasmic trafficking and nuclear import of HIV-1 genomes during infection, PNAS, 2017, Dec 12; 114(50)E10707

Roganowicz MD, Komurlu S, Mukherjee S, Plewka J, Alam SL, Skorupka KA, Wan Y, Dawidowski D, Cafiso DS, Ganser-Pornillos BK, Campbell EM, Pornillos O. TRIM5α SPRY/coiled-coil interactions optimize avid retroviral capsid recognition, PLoS Pathog, 2017 Oct 17; 13(10)e1006686

Flavin W, Bousset L, Green Z, Chu Y, Skarpathiotis S, Chaney M, Kordower J, Melki R, Campbell EM. Endocytic vesicle rupture is a conserved mechanism of cellular invasion by amyloid proteins, Acta Neuropathologica, published online May 19, 2017.

Dharan A, Talley S, Tripathi A, Mamede JI, Majetschak M, Hope TJ, Campbell EM.KIF5B and Nup358 Cooperatively Mediate the Nuclear Import of HIV-1 during Infection. PLoS Pathog. 2016 Jun; 12 (6)e1005700

Imam S, Talley S, Nelson R, Dharan A, O’Connor C, Hope TJ, Campbell EM, TRIM5alpha Degradation via Autophagy Is Not Required for Retroviral Restriction, J Virol, 2016 Jan 13; 90(7):3400-10

Campbell, EM, Hope TJ. HIV-1 capsid: the multifaceted key player in HIV-1 infection. Nat Rev Microbiol. 2015. July 16;13(8)471-83.

Freeman D, Cedillos R, Choyke S, Lukic Z, McGuire K, Marvin S, Burrage A,  M.Sudholt  S, Rana A, O'Connor C, Wiethoff CM, Campbell, EM. Alpha-synuclein induces lysosomal rupture and cathepsin dependent reactive oxygen species following endocytosis PLoS One 2013 May 2, 8:4