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Jürgen Bosch, PhD

Assistant Professor

Departmental Affiliation(s):

Biochemistry and Molecular Biology

Center & Institute Affiliation(s):

Contact Information

615 N. Wolfe Street
Room W8708
Baltimore , Maryland   21205
US        

410-614-4742
410-955-2926

Personal website : http://lupo.jhsph.edu

SciVal Experts Research Profile

Education

PhD , Technical University of Munich , 2003
MS , Technical University of Munich , 1998

Overview

Our current research interest is focused on the Plasmodium parasite, the causative agent of Malaria, leading to 300-500 million infections per year and more than 1.2 million deaths worldwide [Murray et al.,The Lancet (2012) vol. 379 (9814) pp. 413-431].

The complex life cycle of the malaria parasite involves switching between mosquito and human hosts. Plasmodium is thereby constantly threatened by the host immune system, from which it evades by hiding inside of human liver- and red blood-, as well as mosquito midgut cells. This strategy requires the parasite to traverse various host membranes and undergo dramatic conversion processes to accommodate its rapidly changing environment. In my lab, we are interested in the intricate molecular mechanisms underlying these multiple host cell passages and the metabolic conversion processes in between (for more details visit our website at http://lupo.jhsph.edu). 

Using a targeted structure based drug design approach, we employ X-ray crystallography, virtual library screening (VLS), and surface plasmon resonance (SPR) methods to study important key players of these plasmodial mechanisms, with the ultimate aim to develop novel, drug-like compounds to future therapeutic use.

Malaria; crystallography; drug design; Glideosome; Invasion machinery; Egress; Autophagy; Proteases; Surface Plasmon Resonance; SPR; protein protein interaction; FBDD; Fragment Based Drug Design; Interface inhibitors; Biophysics; Biochemistry; Plasmodium; Atg8; Atg3; Atg7; Toxoplasma; Cryptosporidium; structure based drug design; SBDD; Aldolase; MTIP; GAP50

Small molecule drug bound to an essential protein interface of a plasmodial protein. 

Protein crystals