Molecular Mechanisms of Infection and Disease Group

Presentation

Our group is broadly interested in understanding the molecular mechanisms that underlie infectious disease. Current work focuses on:

• Nucleocytoplasmic transport of HIV proteins
• Activation of Epstein-Barr virus lytic infection

The approach is to study the structure and function of key proteins involved in these processes using X-ray crystallography and complementary techniques. The long-term goal is to use the insights gained to develop new medically relevant molecules for the treatment and prevention of disease.

Key Words:
HIV, Epstein-Barr Virus, nuclear transport, lytic replication

Techniques:

• Protein expression and purification
• Biochemical and biophysical characterization of macromolecular complexes
• Electron microscopy (with LMES)
• X-ray crystallography

Publications:
Morinière J, Rousseaux S, Steuerwald U, Soler-López M, Curtet S, Vitte AL, Govin J, Gaucher J, Sadoul K, Hart DJ, Krijgsveld J, Khochbin S, Müller CW and Petosa C. (2009) Cooperative binding of two acetylation marks on a histone tail by a single bromodomain. Nature 461: 664-668

Karlsson QH, Schelcher C, Verrall E, Petosa C, Sinclair AJ. (2008) Methylated DNA recognition during the reversal of epigenetic silencing is regulated by cysteine and serine residues in the Epstein-Barr virus lytic switch protein. PLoS Pathog. 4(3):e1000005.

Petosa C, Morand P, Baudin F, Moulin M, Artero JB, Müller CW. (2006) Structural basis of lytic cycle activation by the Epstein-Barr virus ZEBRA protein. Mol. Cell 21:565-72.

Petosa, C., Schoehn, G., Askjaer, P., Bauer, U., Moulin, M., Steuerwald, U., Soler-López, M., Baudin, F., Mattaj, I.W., Müller, C.W. (2004) Architecture of CRM1/Exportin1 suggests how cooperativity is achieved during formation of a nuclear export complex. Mol. Cell 16:761-775.

(A full list of publications since 2009 is available here)