Prof. Dr. Rita Gerardy-Schahn
| My Research Interest in RESIST |
“Cells from the outside are sugar”. This is a standing rule for which exceptions do not exist. Linked to lipids and proteins at cell surfaces, sugars (glycans) form the outermost front of cells, the glycocalyx, a structure destined to mediate cellular communication in all living systems and, of relevance in RESIST, a structure essentially involved in the control of immune and (by all likelihood 100 %) infection mechanisms. Moreover, glycans present on bacterial cells and/or supplied as food substituents forage the gut microbiome and impact its composition. Finally, secreted glycan polymers form the basis of biofilm matrices used by pathogens to escape therapeutic measures.
Together with researchers in RESIST we will introduce our molecular knowledge on glycosylation enzymes to solve questions of clinical relevance. The long term goal is to establish a rational basis for the design of drugs that would allow destruction of biofilms and prevention of pathogen adhesion – the first step in infection – to mammalian cells.
Prof. Gerardy-Schahn
Prof. Dr. Gerardy-Schahn – Curriculum Vitae
Current Position
Undergraduate and Postgraduate Training
Academic and Research Posts
Other Scientific Roles
Awards and Prizes
Patents
10 Selected Publications
Martin NT, Wrede C, Niemann J, Brooks J, Schwarzer D, Kühnel F, Gerardy-Schahn R. Targeting polysialic acid- abundant cancers using oncolytic adenoviruses with fibers fused to active bacteriophage borne endosialidase. Biomaterials. 2018; 158: 86-94.
Fiebig T, Romano MR, Oldrini D, Adamo R, Tontini M, Brogioni B, Santini L, Berger M, Costantino P, Berti F, Gerardy-Schahn R. An efficient cell free enzyme-based total synthesis of a meningococcal vaccine candidate. NPJ Vaccines 2016; 1: 16017.
Kallolimath S, Castilho A, Strasser R, Grünwald-Gruber C, Altmann F, Strubl S, Galuska CE, Zlatina K, Galuska SP, Werner S, Thiesler H, Werneburg S, Hildebrandt H, Gerardy-Schahn R, Steinkellner H. Engineering of complex protein sialylation in plants. Proc Natl Acad Sci U S A. 2016; 113(34): 9498-503.
Romanow A, Keys TG, Stummeyer K, Freiberger F, Henrissat B, Gerardy-Schahn R. Dissection of hexosyl-and sialyltransferase domains in the bifunctional capsule polymerases from Neisseria meningitidis W and Y defines a new sialyltransferase family. J Bio Chem. 2014; 289(49): 33945-57.
Keys TG, Fuchs HL, Ehrit J, Alves J, Freiberger F, Gerardy-Schahn R. Engineering the product profile of a polysialyltransferase. Nat Chem Biol. 2014; 10(6): 437-42.
Romanow A, Haselhorst T, Stummeyer K, Claus H, Bethe A, Mühlenhoff M, Vogel U, von Itzstein M, Gerardy- Schahn R. Deleterious mutations in LRBA are associated with a syndrome of immune deficiency and autoimmunity. J Biol Chem. 2013; 288(17): 11718-30.
Hildebrandt H, Mühlenhoff M, Oltmann-Norden I, Röckle I, Burkhardt H, Weinhold B, Gerardy-Schahn R. Imbalance of neural cell adhesion molecule and polysialyltransferase alleles causes defective brain connectivity. Brain. 2009; 132(Pt 10): 2831-8.
Eckhardt M, Gotza B, Gerardy-Schahn R. Membrane topology of the mammalian CMP-sialic acid transporter. J Biol Chem. 1999; 274(13):8779-87.
Münster AK, Eckhardt M, Potvin B, Mühlenhoff M, Stanley P, Gerardy-Schahn R. Mammalian cytidine 5’- monophosphate N-acetylneuraminic acid synthetase: a nuclear protein with evolutionarily conserved structural motifs. Proc Natl Acad Sci U S A. 1998; 95(16): 9140-5.
Eckhardt M, Mühlenhoff M, Bethe A, Koopman J, Frosch M, Gerardy-Schahn R. Molecular characterisation of eukaryotic polysialyltransferase-1. Nature. 1995; 373(6516): 715-8.
