Benedikt Diewald


A2 Computational analysis of linear interaction motifs and globular protein interfaces in effector proteins

Principal investigator
Heinrich Sticht

Yves Muller

Comparative Analysis of the Nuclear Egress Complexes of Herpesviruses

The beta-herpesvirus HCMV and the alpha-herpesviruses PRV and HSV-1 use Nuclear Egress Complexes (NEC) to mediate membrane budding with the inner nuclear membrane. These budded perinuclear particles subsequently fuse with the outer nuclear membrane to release capsids into the cytoplasm. The complexes consist of UL50-UL53 in case of HCMV and UL34-UL31 in case of PRV and HSV-1. Although the alpha-herpesviral NECs exhibit high structural similarity to the HCMV NEC the interfaces display a remarkable degree of difference in amino acid composition. Using MD simulations, the interfaces within the NECs will be analyzed to identify which positions are important for the interaction and assess whether the design of a broadly neutralizing anti-herpes agent is viable.

Figure: The sequence alignment displays a high overall sequence identity of PRV (4Z3U) and HSV-1 (4ZXS) UL34 proteins.




October 2016 8th Annual Retreat, Erlangen School of Molecular Communication, Kloster Schloss Schney, Lichtenfels, Germany
“Comparative study of different herpesviral nuclear egress complex interfaces using molecular dynamics”
April 2016 30. Moelcular Modelling Workshop, Erlangen, Germany
"Design of antibody-based peptide inhibitors to disrupt important protein-protein interactions in HIV and HCMV"