Mr. Michael Lenders

Mini Academic CV

University degrees:

First degree or intermediate examination:

  • Bachelor of Science, 2010, Heinrich-Heine Universität, Düsseldorf, Germany

Second degree and/or intermediate examination:

  • Master of Science, 2012, Heinrich-Heine Universität, Düsseldorf, Germany


  • Schwarz CKW, Lenders MHH, Smits SHJ, Schmitt L. (2012) Secretion of slow-folding proteins by a Type 1 Secretion System, Bioengineered (3) 5, 1-4.
  • Schwarz CK, Landsberg CD, Lenders MH, Smits SH, Schmitt L. (2012) Using an E. coli Type 1 secretion system to secrete the mammalian, intracellular protein IFABP in its active form. J Biotechnol. Feb 17.


BioStruct PhD project

The membrane fusion protein HlyD from E. coli

Many Gram-negative bacteria secrete toxins, lipases, haem-binding proteins or S-layer protein through a Type I secretion system (T1SS). The paradigm of a T1SS is the haemolysin A (HlyA) secretion machinery of E. coli that is, like all T1SS, composed of an ABC transporter (HlyB) and a membrane fusion protein (MFS, HlyD) both located in the inner membrane as well as an outer membrane protein (TolC). The substrate, HlyA, a 1023 amino acid toxin, is secreted in one step across both membranes of E. coli through a channel-tunnel composed of these three membrane proteins thereby preventing any periplasmic intermediate. Here, the MFS which forms a complex with the ABC transporter HlyB in the inner membrane of E. coli seems to play a pivotal role – in the presence of the substrate, HlyD recruits the outer membrane protein TolC by an unknown mechanism. Although various crystal structures of MFS have been determined (AcrA, MexA, ), HlyD is the exception since none of the MFS analyzed so far is involved in a T1SS or contains a single transmembrane helix including a short cytoplasmic tail.
Based on an initial overexpression protocol, the projects aims to elucidate the oligomeric state of HlyD, its three-dimensional structure and potential interaction sites of HlyD with the substrate (HlyA), the ABC transporter (HlyB) and the outer membrane protein (TolC).


Topic Supervisor:

undefined Prof. Dr. Lutz Schmitt, Institute for Biochemistry, Heinrich Heine University Duesseldorf, Schmitt Group

Complementary Supervisor:

undefinedProf. Dr. Georg Groth, Institute for Plant Biochemistry, Heinrich Heine University Duesseldorf, Groth Group

Responsible for the content: E-MailBioStruct Office