Angelika Gründling is a Professor in Molecular Microbiology at Imperial College London, where she started her independent research career in 2007. The research focuses onthe investigation of fundamental processes that are essential for the growth of Gram-positive bacterial pathogens. She combines genetic, biochemical and in collaborations structural approaches to provide mechanistic insight into cell wall synthesis and nucleotide signalling pathways in Staphylococcus aureus and Listeria monocytogenes.Angelika obtained her Ph.D. in Microbiology from the University of Vienna in 2000. She performed her postdoctoral training at the Harvard Medical School, where she investigated flagallar motility in the bacterial pathogen Listeria monocytogenes and at the University of Chicago, where she initiated her studies on the cell wall of S. aureus. At Imperial College London she continues her work on the bacterial cell wall and more recently on the essential signalling nucleotide c-di-AMP.
et al., 2020, GtcA is required for LTA glycosylation in Listeria monocytogenes serovar 1/2a and Bacillus subtilis, The Cell Surface, Vol:6, ISSN:2468-2330
et al., 2020, Phosphoglycerol-type wall and lipoteichoic acids are enantiomeric polymers differentiated by the stereospecific glycerophosphodiesterase GlpQ (vol 295, pg 4024, 2020), Journal of Biological Chemistry, Vol:295, ISSN:0021-9258, Pages:8873-8873
et al., 2020, Identification of the main glutamine and glutamate transporters in Staphylococcus aureus and their impact on c-di-AMP production, Molecular Microbiology, Vol:113, ISSN:0950-382X, Pages:1085-1100
et al., 2020, High‐throughput transposon sequencing highlights the cell wall as an important barrier for osmotic stress in methicillin resistant Staphylococcus aureus and underlines a tailored response to different osmotic stressors, Molecular Microbiology, Vol:113, ISSN:0950-382X, Pages:699-717
et al., 2020, Phosphoglycerol-type wall- and lipoteichoic acids are enantiomeric polymersdifferentiated by the stereospecific glycerophosphodiesterase GlpQ, Journal of Biological Chemistry, Vol:12, ISSN:0021-9258, Pages:4024-4034