Project Description
Public­ations

TP03A: A Dynamics of hepatitis B virus morphogenesis in persistent infection

In the serum of patients chronically infected with hepatitis B virus one does not only find complete DNA-containing virions, but also virions harbouring “empty” or RNA-containing capsids, respectively. The proportion of these non-canonical forms of virions varies drastically depending on the intrahepatic viral replication activity and the treatment status, and might be relevant for the continuous stimulation of the host immune response responsible for long-term liver inflammation ultimately resulting in cirrhosis and hepatocellular carcinoma.
Seitz S, Iancu C, Volz T, Mier W, Dandri M, Urban S, Bartenschlager R. 2016. A slow maturation process renders hepatitis B virus infectious. Cell Host Microbe. 20:25-35
Seitz S, Urban S, Antoni C, Böttcher B. 2007. Cryo-electron microscopy of hepatitis B virions reveals variability in envelope capsid interactions. EMBO J. 26:4160-4167.
Lauber C, Seitz S, Mattei S, Suh A, Beck J, Herstein J, Börold J, Salzburger W, Kaderali L, Briggs J, Bartenschlager R. 2017. Deciphering the origin and evolution of hepatitis B viruses by means of a family of nonenveloped fish viruses. Cell Host Microbe. 22:387-399.e6.
Binder M, Eberle F, Seitz S, Mücke N, Hüber CM, Kiani N, Kaderali L, Lohmann V, Dalpke A, Bartenschlager R. 2011. Molecular mechanism of signal perception and integration by the innate immune sensor retinoic acid-inducible gene-I (RIG-I). J Biol Chem. 286:27278-87.
Petersen J, Dandri M, Mier W, Lütgehetmann M, Volz T, von Weizsäcker F, Haberkorn U, Fischer L, Pollok JM, Erbes B, Seitz S, Urban S. 2008. Prevention of hepatitis B virus infection in vivo by entry inhibitors derived from the large envelope protein. Nat Biotechnol. 26:335-341.
Corcuera A, Stolle K, Hillmer S, Seitz S, Lee JY, Bartenschlager R, Birkmann A, Urban A. 2018. Novel non-heteroarylpyrimidine (HAP) capsid assembly modifiers have a different mode of action from HAPs in vitro. Antiviral Res. 158:135-142.
Schuetz AK, Hornemann, S, Wälti, MA, Greuter, L, Tiberi, C, Cadalbert, R, Ganter, M, Riek, R, Hammarström, P, Nilsson, KPR, Böckmann, A, Aguzzi, AA, Meier, BH. 2018. Binding of polythiophenes to amyloids: structural mapping of the pharmacophore. ACS Chem Neurosci. 9:475-481.
Schütz, AK, Kay, LE 2016. A dynamic molecular basis for malfunction in disease mutants of p97/VCP, eLife. 5:e20143.
Schütz, AK, Vagt, T, Huber, M, Ovchinnikova, OY, Cadalbert, R, Wall, J, Güntert, P, Böckmann, A, Glockshuber, R, Meier, BH. 2015. Atomic-resolution three-dimensional structure of amyloid β fibrils bearing the Osaka mutation. Angewandte Chemie. 54:331-335.
Herrmann, US, Schütz, AK, Shirani, H, Huang, D, Saban, D, Nuvolone, M, Li, B, Ballmer, B, Åslund, AK, Mason, JJ, Rushing, E, Budka, H, Nyström, S, Hammarström, P, Böckmann, A, Caflisch, A, Meier, BH, Nilsson, KP, Hornemann, S, Aguzzi, A. 2015. Structure-based drug design identifies polythiophenes as antiprion compounds. Science Translational Medicine. 7(299):ra123.