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Prof. Dr. Leonhard Möckl

  • Professorship for Nano-optical Imaging
  • Associated Group Leader
  • Room A.3.428
  • Phone +49 9131 7133115
  • Email
  • Head of research group Physical Glycosciences

Leonhard Möckl studied Chemistry and Biochemistry at LMU Munich. He obtained his PhD in 2015 with a thesis on the role of the glycocalyx in membrane protein organization. In 2016, he joined the lab of W.E. Moerner at Stanford University, where he used single-molecule techniques to investigate the glycocalyx and furthermore developed deep-learning based approaches for single-molecule studies. In 2020, he joined the MPL as an independent group leader. Since 2024, he holds the professorship for Nano-optical Imaging at FAU, located at the newly established CITABLE.

In his free time, he loves to read, to play the piano, to hike, and to play 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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