Ms. Iris Gawarzewski

Schmitt Group Institute for Biochemistry Heinrich Heine University Universitätsstr.1, Geb. 26.42.02 R.12 40225 Düsseldorf, Germany  +49(0)211-81-10774

Mini Academic CV

University degrees:

First degree or intermediate examination:

• Vordiplom (Biology) 2006 HHU Düsseldorf

Second degree and/or intermediate examination:

• Diplom (Biology) 2009 HHU Düsseldorf

Prices/Scholarships:

• Dr. Walter Haaß-Price

BioStruct PhD project

Determination of the AIDA-I β-barrel crystal structure: getting the clue to the autotransporter secretion pathway.
In the group of Prof. Jose, a surface display system for recombinant proteins has been developed which is named Autodisplay. It can be used for the efficient surface display of recombinant proteins, including enzymes, antibodies, receptors or small protein drugs on E. coli. Autodisplay is based on the secretion mechanism of the autotransporter proteins, a large family of self-translocating proteins in gram-negative bacteria. The crucial part of this secretion mechanism is a porin-like β-barrel structure, responsible for outer membrane translocation of the passenger domain. In autodisplay this beta-barrel is derived from the natural E. coli autotransporter protein AIDA-I. In developing and optimizing the autodisplay system, we found a way to overexpress the β-barrel of AIDA-I within the outer membrane of E. coli, up to an amount, which is in the same order of magnitude as the natural outer membrane proteins OmpA or OmpF/C. The aim of the present project is
a) to use this method of overexpression for purification of the β-barrel of AIDA-I and to create crystals as the basis for a structural model and
b) to verify this model by functional studies.

Topic Supervisor: Prof. Dr. Joachim Jose, Institute of Pharmaceutical and Medicinal Chemistry, Jose Group

Complementary Supervisor: Prof. Dr. Lutz Schmitt, Institute for Biochemistry, Schmitt Group

BioStruct Fellow: Ms. Iris Gawarzewski