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Research group Dr. phil. nat. Christian Schölz

Proteomics of Virus-Host interaction

Areas of investigation / research topics

The Human immunodeficiency virus (HIV) consists of a small genome and thus relies heavily on the host cellular machinery for production of viral progeny. To exploit cellular proteins for replication and to overcome host cellular factors with antiviral activity, HIV has evolved a set of accessory and regulatory proteins that apparently shape an optimized environment for its replication and facilitate evasion from innate immunity, respectively. Over the past few years it has become clear that many viruses can induce post-translational modifications (PTMs) of the host cell environment at multiple levels to manipulate important cellular signaling pathways that affect e.g. cell cycle control, protein degradation, transcription, and translation. Modifications include phosphorylation, glycosylation, ubiquitination, methylation and all kinds of acylations.
However, only little is known about the specific cellular targets of PTMs in the context of viral infection. Gaining more detailed insights into the underlying mechanisms and their effects on viral transcription/latency as well as their effect on viral restriction will help to better understand the molecular biology of HIV itself and provide a basis for the development of new therapeutic tools.

Workflow of PTM analysis.
Schematic overview of the required steps during analysis of post-translational modified proteins. Shown here is a SILAC approach, where stable isotope labeled amino acids are used for labeling of proteins during cell culture phase. Alternatively, cells can be grown without isotope labeling and derived proteins/peptides are labeled subsequently by isobaric mass tag technology (TMT). Identified Targets are further analyzed and validated.

Recently, the proteome-wide analysis of PTMs was developed, allowing for the first time broad-range and unbiased investigations of changes in the global PTM landscape. Moreover, new and sensitive methods for label-free quantitative interaction proteomics in primary cells have become available, which permit detection also of weak interactors with spatial and temporal resolution.
The group seeks to identify new virus-host interactions, established during the viral lifecycle, focusing mainly, but not exclusively, on HIV infection. Using several techniques ranging from classical cell biological and biochemical methods towards state-of-the art analysis by e.g. mass spectrometry, we try to identify and characterize novel protein-protein interactions that are essential for viral progeny or the immunological surveillance. Identified targets will be analyzed in more detail to understand their function within the context of infection.

Current Group Members

Christian Schölz
, PhD
Email: schoelz(at)mvp.uni-muenchen.de
Phone: +49 89 2180 78010

Lin Chen, PhD Student
Email: chen(at)mvp.uni-muenchen.de
Phone: +49 89 2180 78123

Jonathan Schneider, BSc, internship
Phone: +49 89 2180 78123

Franziska Sippl, BSc, internship
Phone: +49 89 2180 78123

Former lab members

Tobias Klötzler
Corinna Biermeier

Selected publications

Schölz C, Lyon D, Refsgaard JC, Jensen LJ, Choudhary C, Weinert BT; “Avoiding abundance bias in the functional annotation of post-translationally modified proteins”; Nature Methods 2015, 1003-1004

Schölz C, Weinert BT, Wagner SA, Beli P, Yasuyuki M, Qi J, Jensen LJ, Streicher W, McCarthy AR, Westwood NJ, Lain S, Cox J, Matthias P, Mann M, Bradner JE & Choudhary C; “Acetylation site specificities of lysine deacetylase inhibitors in human cells”; Nature Biotechnology 2015, 415-423

Weinert BT, Iesmantavicius V, Moustafa T, Schölz C, Wagner SA, Magnes C, Zechner R, Choudhary C.; “Acetylation dynamics and stoichiometry in Saccharomyces cerevisiae”; Molecular Systems Biology 2014, 10:716

Weinert BT, Schölz C, Wagner SA, Iesmantavicius V, Su D, Daniel JA, Choudhary C; “Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation”, Cell Reports 2013, 842-851

Weinert  BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C; “Acetyl-Phosphate is a Critical Determinant of Lysine Acetylation in E. coli”; Molecular Cell, 2013, 265-272

Contact

Dr. Christian F. Schölz
Max von Pettenkofer Institute, Virology
National Reference Center for Retroviruses
Faculty of Medicine
LMU München
Feodor-Lynen-Str. 23
81377 München

Tel.: +49 89 2180 78010
E-mail.: schoelz(at)mvp.uni-muenchen.de