Martin Grießl

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A3 Structural basis for the interaction between potyviral capsid proteins and plant chaperones

Principal investigator
Yves Muller

Mentor
Uwe Sonnewald

PhD exam: 13.06.2013

Structural basis for the interaction between potyviral capsid proteins and plant chaperones

Potyviruses are the largest family of plant viruses and infect a huge number of agricultural crops. As a prerequisite for potyvirus propagation in plants, the viral coat protein (CP) acts as movement protein that permits infectious virions intra- and intercellular trafficking by recruiting host factors. Recently, it was shown that potyviruses had to interact with specific plant Hsp40 chaperones for this assignment. In Nicotiana tabacum they referred this chaperones as “Nicotiana tabacum coat protein interacting proteins” (NtCPIPs). Our aim is to elucidate the atomic determinants of the interaction between the viral CP and the plant chaperones from the host by means of protein crystallography. Until now we were successful in producing and purifying different variants of the CP and NtCPIPs. Furthermore, we succeeded in crystallizing a deletion variant of a plant chaperone, but these crystals did not diffract to adequate resolution. To unravel any structural changes upon binding we not only want to characterize the proteins alone, but also in complex with each other. We were able to coexpress and copurify the potato virus Y coat protein (PVY-CP) together with a member of the chaperone family. Extensive crystallization trials are currently being set up.

Figure: Model of replication and cell-to-cell transfer of potyviral genome in plants. Newly synthesized genomes associate with coat proteins (CP) to form a virion or a ribonucleoprotein complex. This virion or complex interacts with a channel formed by Cl proteins associated with plasmodesmata. The virion or complex is transported through the channel and the plasmodesma in the adjacent plant cell. CW: cell wall, ER: endoplasmic reticulum, PD plasmodesma.

 

Publications

Griessl, M. H., Jungkunz, I., Sonnewald, U. and Muller, Y. A. (2012). Purification crystallization and preliminary X-ray diffraction analysis of the Hsp40 protein CPIP1 from Nicotiana tabacum. Acta Crystallogr Sect F Struct Biol Cryst Commun 68, 236-239.

Sturm, K. U., Griessl, M. H., Wagner, C., Deiwick, J., Hensel, M. and Muller, Y. A. (2011). Crystallization and preliminary crystallographic analysis of an Ig-domain-encompassing fragment of the giant adhesion protein SiiE from Salmonella enterica. Acta Crystallogr Sect F Struct Biol Cryst Commun 67, 1371-1374.

 

Presentations

July 2012 4th Annual Retreat, Erlangen School of Molecular Communication, Kloster Banz, Bad Staffelstein, Germany
Structural basis of pathogen-host interactions
Poster
     
October 2011 First International SFB 796 Conference: Mechanisms of viral host cell manipulations: from plants to humans, Bamberg, Germany
Structural bais for the interaction between potyviral capsid proteins and plant chaperones
Poster
     
September 2011 14th Heart of Europe bio-Crystallography Meeting, Z.agan', Poland
SiiE: insights into a giant 5559 amino acids adhesin of Salmonella enterica
Talk
     
July 2011 3rd Annual Retreat, Erlangen School of Molecular Communication, Kloster Banz, Bad Staffelstein, Germany
Structural analysis of CPIP1 from Nicotiana tabacum and SiiE from Salmonella enterica
Talk and Poster
     
September 2010 2nd Annual Retreat, Erlangen School of Molecular Communication, Kloster Banz, Bad Staffelstein, Germany
Structural basis for the interaction between potyviral capsid proteins and plant chaperones
Talk
     
September 2009 First Annual Retreat, Erlangen School of Molecular Communication, Schloss Atzelsberg, Atzelsberg, Germany
Structural basis for the interaction between potyviral capsid proteins and plant chaperones
Talk
     
March 2009 17. Jahrestagung der Deutschen Gesellschaft für Kristallographie, Hannover, Germany
Structural basis for the interaction between potyviral capsid proteins and plant chaperones
Poster

 

Awards

Cooperation Award together with Arne Berthelmann and Kristin Kaßler
3rd Annual Retreat of the Erlangen School of Molecular Communication, Kloster Banz, Bad Staffelstein, Germany, July 2011
"Strukturelle Aufklärung der Bindung zwischen dem potyviralen Hüllprotein PVY-CP und seinem zellulären Interaktionspartner aus N. tabacum." .