Viruses depend on their hosts to copy themselves and spread. Upon infection, a virus will hijack the host machinery to replicate its genome, manufacture its proteins and assemble new viral particles. The host in defence deploys its own weapons against the virus in an attempt to combat the infection. This host defence depends on an intricate signaling chain that activates the host’s immune system. One tactic employed by viruses to enhance their replication and thwart the immune reaction is to interfere with this signaling mechanism. New research from the lab of Tim Skern and their collaborators from the University of Queensland (Australia) now shows how the vaccinia virus protein A46 disrupts immune signaling by jamming the cellular transmission chain. The paper is now online in the journal “Structure”.
The 2020 Nobel Prize for Chemistry is awarded to Emmanuelle Charpentier and Jennifer Doudna for their groundbreaking discoveries on the CRISPR/Cas9 system, a now widely used genome editing tool that has revolutionized biomedicine. Emmanuelle Charpentier was a principal investigator at the Max Perutz Labs at the University of Vienna from 2002 to 2009, where she laid the groundwork for developing the CRISPR/Cas9 technology. The Max Perutz Labs together with the University of Vienna congratulate Prof. Charpentier on this outstanding achievement.
In a project supported by the Volkswagen foundation, the lab of Bojan Zagrovic and their collaborators Zoya Ignatova (University of Hamburg) and Markus Zweckstetter (MPI Biophysical Chemistry Göttingen) aim at experimentally and computationally testing the mRNA-protein complementarity hypothesis. This novel and still controversial idea could help explain the origin of the universal genetic code, but may also carry major implications for the biology of today. The grant amounts to a total of €1.5 m and is coordinated by Zoya Ignatova.
The Aligning Science Across Parkinson’s Initiative (ASAP) has awarded a grant to Sascha Martens’ group and scientists from the University of Pennsylvania, Monash University and MPI for Biophysics in Frankfurt. The project is coordinated by James Hurley from the University of California Berkeley. The project is endowed with USD 7.000.000 and will reveal the mechanisms of mitophagy and its involvement in Parkinson’s Disease.
Autophagy, from the Greek for ‘self-eating’, is an essential process that isolates and recycles cellular components under conditions of stress or when resources are limited. Cargoes such as misfolded proteins or damaged organelles are captured in a double membrane-bound compartment called the autophagosome and targeted for degradation. A fundamental question concerns precisely how these “garbage bags” form in the cell. Scientists led by Sascha Martens from the Max Perutz Labs, a joint venture of the University of Vienna and the Medical University of Vienna, have now reconstructed the first steps in the formation of autophagosomes. They show that tiny vesicles loaded with the protein Atg9 act as the seed from which the autophagosome emerges. The study is published in Science.
The group of Kristina Djinovic-Carugo has revealed the molecular structure of a calcium-regulated form of the protein α-actinin, and has elucidated the mechanism of how calcium binds and regulates it. In α-actinin from the parasite E. histolytica, calcium binding triggers an increase in protein rigidity, which impairs its ability to bundle actin filaments. The study is published in PNAS and could help understand calcium regulation in human forms of α-actinin. The mechanism may also provide guidance for the development of novel therapeutics to treat amoebic dysentery caused by E. histolytica that threatens millions of people in developing countries every year.
The Max Perutz Labs are embedded in the Vienna Biocenter, providing access to outstanding core facilities shared by all members of the campus in addition to facilities unique to our institute.
With a strong molecular focus and a diversity of model organisms, we aim to bridge basic research with biomedicine.
To honour an extraordinary teacher and scientist, the Max Perutz Labs were named after Max Ferdinand Perutz, who, together with John C. Kendrew, was awarded the 1962 Nobel Prize in Chemistry for his studies on the structure of globular proteins ...
The Max Perutz Labs seek to educate students to think critically and analytically, challenge them to set ambitious goals, and instill in them both broad horizons and deep understanding. In doing so, we aspire to furnish them with the necessary knowledge and skills to push forward the frontiers of 21st century biomedical science.