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  4. Leonhard Möckl

Prof. Dr. Leonhard Möckl

Leonhard Möckl studierte Chemie und Biochemie an der LMU München. Er promovierte 2015 mit einer Arbeit über die Rolle der Glycocalyx in der Organisation von Membranproteinen. Im Jahr 2016 wechselte er in das Labor von W.E. Moerner an der Stanford University, wo er Einzelmolekültechniken zur Untersuchung der Glycocalyx einsetzte und darüber hinaus Deep-Learning-basierte Ansätze für Einzelmolekülstudien entwickelte. Im Jahr 2020 wurde unabhängiger Gruppenleiter am MPL. Seit 2024 hat er die Professur für Nano-optische Bildgebung an der FAU inne, die am neu gegründeten CITABLE angesiedelt ist.

In seiner Freizeit liest er, spielt Klavier, wandert oder spielt Volleyball.

2021

Discovery of indole-modified aptamers for highly specific recognition of protein glycoforms

Alex M. Yoshikawa, Alexandra Rangel, Trevor Feagin, Elizabeth M. Chun, Leighton Wan, Anping Li, Leonhard Möckl, Diana Wu, Michael Eisenstein, et al.

Nature Communications 12 7106 (2021) | Journal | PDF

Glycosylation is one of the most abundant forms of post-translational modification, and can<br>have a profound impact on a wide range of biological processes and diseases. Unfortunately,<br>efforts to characterize the biological function of such modifications have been greatly<br>hampered by the lack of affinity reagents that can differentiate protein glycoforms with robust<br>affinity and specificity. In this work, we use a fluorescence-activated cell sorting (FACS)-<br>based approach to generate and screen aptamers with indole-modified bases, which are<br>capable of recognizing and differentiating between specific protein glycoforms. Using this<br>approach, we were able to select base-modified aptamers that exhibit strong selectivity for<br>specific glycoforms of two different proteins. These aptamers can discriminate between<br>molecules that differ only in their glycan modifications, and can also be used to label gly-<br>coproteins on the surface of cultured cells. We believe our strategy should offer a generally-<br>applicable approach for developing useful reagents for glycobiology research.

Genome-wide CRISPR screens reveal a specific ligand for the glycan-binding immune checkpoint receptor Siglec-7

Simon Wisnovsky, Leonhard Möckl, Stacy A. Malaker, Kayvon Pedram, Gaelen T. Hess, Nicholas M. Riley, Melissa A. Gray, Benjamin A. H. Smith, Michael C. Bassik, et al.

Proceedings of the National Academy of Sciences of the United States of America 118 (5) e2015024118 (2021) | Journal | PDF

Glyco-immune checkpoint receptors, molecules that inhibit immune cell activity following binding to glycosylated cell-surface<br>antigens, are emerging as attractive targets for cancer immunotherapy.<br>Defining biologically relevant ligands that bind and activate such receptors, however, has historically been a significant challenge. Here, we present a CRISPRi genomic screening strategy that allowed unbiased identification of the key genes required for<br>cell-surface presentation of glycan ligands on leukemia cells that bind the glyco-immune checkpoint receptors Siglec-7 and Siglec-9.<br>This approach revealed a selective interaction between Siglec-7 and the mucin-type glycoprotein CD43. Further work identified a specific N-terminal glycopeptide region of CD43 containing clusters of disialylated O-glycan tetrasaccharides that form specific Siglec-7 binding motifs. Knockout or blockade of CD43 in leukemia<br>cells relieves Siglec-7-mediated inhibition of immune killing activity.<br>This work identifies a potential target for immune checkpoint blockade therapy and represents a generalizable approach to dissection of glycan–receptor interactions in living cells.

Here you can download Leonhard's CV.

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