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Professor Waldemar Vollmer
Professor

Waldemar Vollmer

Email: 
Phone: 
+61 7 334 62055

Overview

Background

Overview

Professor Waldemar Vollmer is a microbiologist working on the structure and biogenesis of the bacterial cell wall in various model bacteria and a range of pathogenic and environmental bacteria. He is particularly interested in how bacteria enlarge their cell wall when they grow and divide, and how antibiotics inhibit cell wall synthesis to kill bacteria. Antimicrobial resistance (AMR) is a global problem that is predicted to claim 10 million lives annually by the year 2050 if no new antibiotics are developed. Currently the pipeline of antibiotic development is almost empty and mostly limited to slightly modified versions to existing antibiotics. Professor Vollmer addresses the problem of AMR by generating tailored assays for the development of novel antibiotics that target AMR bacteria.

Collaborations: Professor Vollmer collaborates world-wide with more than 50 researchers at top national and international institutions on cell wall topics in over 30 different bacteria. These topics include: structure and composition of the cell wall and its role in maintaining cell morphology; molecular mechanisms of cell envelope biogenesis; role of new cell wall modifying enzymes in the interaction of pathogenic bacteria with components of the immune system; mechanisms of antibiotic resistance and targeting of cell wall biogenesis by new antibiotics.

Funding and Publications: Professor Vollmer has been awarded more than $15 million funding from research councils and charities in Germany, UK, Europe and USA. He has published more than 200 articles in international journals and has been recognised as a Highly Cited Researcher in Microbiology.

Honours and Awards: Professor Vollmer has been elected to Fellow of the American Academy of Microbiology (2014) and European Academy of Microbiology (2018). He received the annual Academic Distinction Awards from the Vice Chancellor of Newcastle University (2014), has been awarded a Distinguished Scientist Visiting Scholarships at Ben-Gurion University of the Negev (Israel, 2012) and a Visiting Professorship at the University of Cagliari (Italy, 2015), and won a Wellcome Trust Senior Investigator Award (2014). He has co-organised the 2018 Gordon Conference (GRC) "Bacterial Cell Surfaces" (Mt Snow, USA) and the 2016 EMBO Workshop "Bacterial Cell Division: Orchestrating the Ring Cycle" (Prague, Czech Republic).

Short Biography: Prof Waldemar Vollmer has studied chemistry at the University of Applied Sciences in Reutlingen (Germany) and University of Basel (Switzerland). In 1998 he obtained a PhD degree (Dr.rer.nat.) from the University of Tübingen (Germany) for his work on cell wall synthesis in the model bacterium Escherichia coli undertaken at the Max Planck Institute for Developmental Biology. During his postdoctoral studies at the Rockefeller University (New York, USA) he discovered novel cell wall enzymes that are crucial for the virulence of the pathogenic bacterium Streptococcus pneumoiae. In 2003 he was appointed Assistant Professor at the University of Tübingen and moved 2007 to the Centre for Bacterial Cell Biology at Newcastle University (UK), where he worked as Professor of Bacterial Biochemistry on various bacterial cell wall topics in a range of different bacteria. Since April 2023 he is Professorial Research Fellow and Group Leader at the Centre for Superbug Solutions, Institute for Molecular Bioscience (IMB) at the University of Queensland.

Availability

Professor Waldemar Vollmer is:
Available for supervision

Fields of research

Research impacts

Professor Vollmer's basic research on the bacterial cell envelope has led to key advances in our understanding of bacterial cell function and has discovered molecular mechanisms that can be exploited for antibiotic development.

Key research outputs: Prof Vollmer's group has discovered mechanisms of PG biosynthesis and its regulation, novel cell wall enzymes, and mechanisms of coordination between PG synthesis and outer membrane biogenesis. These discoveries provided the first molecular insights into how bacteria robustly maintain, enlarge and modify their cell envelope when they propagate in diverse environments and under stress conditions, and when exposed to antibiotics.

Key capabilities: Prof Vollmer's group is expert in the analysis of the composition of peptidoglycan, the key shape-maintaining and stress-bearing component of the bacterial cell envelope. They also discover new cell wall enzymes and study the activities and interactions of of key cell wall synthases and hydrolases (lysins or autolysins). They are also expert in determining the cleavage site of cell wall-degrading lysins and establishing biochemical assays for cell wall enzymes, for studying their inhibition by antibiotics. They combine their molecular biology work with studies on the physiology of bacterial cells impaired in cell wall biogenesis.

Works

Search Professor Waldemar Vollmer’s works on UQ eSpace

239 works between 1993 and 2024

221 - 239 of 239 works

2005

Journal Article

Listeria monocytogenes EGD lacking penicillin-binding protein 5 (PBP5) produces a thicker cell wall

Korsak, Dorota, Vollmer, Waldemar and Markiewicz, Zdzislaw (2005). Listeria monocytogenes EGD lacking penicillin-binding protein 5 (PBP5) produces a thicker cell wall. FEMS Microbiology Letters, 251 (2), 281-288. doi: 10.1016/j.femsle.2005.08.009

Listeria monocytogenes EGD lacking penicillin-binding protein 5 (PBP5) produces a thicker cell wall

2005

Journal Article

Crystal structure of MltA from Escherichia coli reveals a unique lytic transglycosylase fold

van Straaten, Karin E., Dijkstra, Bauke W., Vollmer, Waldemar and Thunnissen, Andy-Mark W.H. (2005). Crystal structure of MltA from Escherichia coli reveals a unique lytic transglycosylase fold. Journal of Molecular Biology, 352 (5), 1068-1080. doi: 10.1016/j.jmb.2005.07.067

Crystal structure of MltA from Escherichia coli reveals a unique lytic transglycosylase fold

2005

Journal Article

Susceptibility to antibiotics and beta-lactamase induction in murein hydrolase mutants of Escherichia coli

Korsak, Dorota, Liebscher, Sylvia and Vollmer, Waldemar (2005). Susceptibility to antibiotics and beta-lactamase induction in murein hydrolase mutants of Escherichia coli. Antimicrobial Agents and Chemotherapy, 49 (4), 1404-1409. doi: 10.1128/AAC.49.4.1404-1409.2005

Susceptibility to antibiotics and beta-lactamase induction in murein hydrolase mutants of Escherichia coli

2005

Journal Article

Why are pathogenic staphylococci so lysozyme resistant? The peptidoglycan O-acetyltransferase OatA is the major determinant for lysozyme resistance of Staphylococcus aureus

Bera, Agnieszka, Herbert, Silvia, Jakob, Andreas, Vollmer, Waldemar and Gotz, Friedrich (2005). Why are pathogenic staphylococci so lysozyme resistant? The peptidoglycan O-acetyltransferase OatA is the major determinant for lysozyme resistance of Staphylococcus aureus. Molecular Microbiology, 55 (3), 778-787. doi: 10.1111/j.1365-2958.2004.04446.x

Why are pathogenic staphylococci so lysozyme resistant? The peptidoglycan O-acetyltransferase OatA is the major determinant for lysozyme resistance of Staphylococcus aureus

2004

Journal Article

Murein (peptidoglycan) binding property of the essential cell division protein FtsN from Escherichia coli

Ursinus, Astrid, van den Ent, Fusinita, Brechtel, Sonja, de Pedro, Miguel, Holtje, Joachim-Volker, Lowe, Jan and Vollmer, Waldemar (2004). Murein (peptidoglycan) binding property of the essential cell division protein FtsN from Escherichia coli. Journal of Bacteriology, 186 (20), 6728-6737. doi: 10.1128/JB.186.20.6728-6737.2004

Murein (peptidoglycan) binding property of the essential cell division protein FtsN from Escherichia coli

2004

Journal Article

The architecture of the murein (peptidoglycan) in gram-negative bacteria: Vertical scaffold or horizontal layer(s)?

Vollmer, Waldemar and Holtje, Joachim-Volker (2004). The architecture of the murein (peptidoglycan) in gram-negative bacteria: Vertical scaffold or horizontal layer(s)?. Journal of Bacteriology, 186 (18), 5978-5987. doi: 10.1128/JB.186.18.5978-5987.2004

The architecture of the murein (peptidoglycan) in gram-negative bacteria: Vertical scaffold or horizontal layer(s)?

2003

Journal Article

Overproduction of inactive variants of the murein synthase PBP1B causes lysis in Escherichia coli

Meisel, Ute, Holtje, Joachim-Volker and Vollmer, Waldemar (2003). Overproduction of inactive variants of the murein synthase PBP1B causes lysis in Escherichia coli. Journal of Bacteriology, 185 (18), 5342-5348. doi: 10.1128/JB.185.18.5342-5348.2003

Overproduction of inactive variants of the murein synthase PBP1B causes lysis in Escherichia coli

2002

Journal Article

Peptidoglycan N-acetylglucosamine deacetylase, a putative virulence factor in Streptococcus pneumoniae

Vollmer, Waldemar and Tomasz, Alexander (2002). Peptidoglycan N-acetylglucosamine deacetylase, a putative virulence factor in Streptococcus pneumoniae. Infection and Immunity, 70 (12), 7176-7178. doi: 10.1128/IAI.70.12.7176-7178.2002

Peptidoglycan N-acetylglucosamine deacetylase, a putative virulence factor in Streptococcus pneumoniae

2002

Book Chapter

Murein (Peptidoglycan)

Heidrich, C. and Vollmer, W. (2002). Murein (Peptidoglycan). Biopolymers, Polysaccharides I: Polysaccharides from Prokaryotes. (pp. 431-463) edited by Alexander Steinbüchel, Erick J. Vandamme, Martin Hofrichter and Sophie De Baets. Weinheim, Germany: Wiley.

Murein (Peptidoglycan)

2001

Journal Article

Morphogenesis of Escherichia coli

Vollmer, Waldemar and Holtje, Joachim-Volker (2001). Morphogenesis of Escherichia coli. Current Opinion in Microbiology, 4 (6), 625-633. doi: 10.1016/S1369-5274(01)00261-2

Morphogenesis of Escherichia coli

2001

Journal Article

Identification of the teichoic acid phosphorylcholine esterase in Streptococcus pneumoniae

Vollmer, Waldemar and Tomasz, Alexander (2001). Identification of the teichoic acid phosphorylcholine esterase in Streptococcus pneumoniae. Molecular Microbiology, 39 (6), 1610-1622. doi: 10.1046/j.1365-2958.2001.02349.x

Identification of the teichoic acid phosphorylcholine esterase in Streptococcus pneumoniae

2001

Book Chapter

A multienzyme complex involved in murein synthesis of Escherichia coli

von Rechenberg, M., Vollmer, W. and Höltje, J.V. (2001). A multienzyme complex involved in murein synthesis of Escherichia coli. Microbial fundamentals of biotechnology. (pp. 249-262) edited by Volkmar Braun and Friedrich Götz. Weinheim, Germany: Wiley.

A multienzyme complex involved in murein synthesis of Escherichia coli

2000

Journal Article

The pgdA gene encodes for a peptidoglycan N-acetylglucosamine deacetylase in Streptococcus pneumoniae

Vollmer, Waldemar and Tomasz, Alexander (2000). The pgdA gene encodes for a peptidoglycan N-acetylglucosamine deacetylase in Streptococcus pneumoniae. Journal of Biological Chemistry, 275 (27), 20496-20501. doi: 10.1074/jbc.M910189199

The pgdA gene encodes for a peptidoglycan N-acetylglucosamine deacetylase in Streptococcus pneumoniae

2000

Journal Article

A simple screen for murein transglycosylase inhibitors

Vollmer, Waldemar and Holtje, Joachim-Volker (2000). A simple screen for murein transglycosylase inhibitors. Antimicrobial Agents and Chemotherapy, 44 (5), 1181-1185. doi: 10.1128/AAC.44.5.1181-1185.2000

A simple screen for murein transglycosylase inhibitors

1999

Journal Article

Demonstration of molecular interactions between the murein polymerase PBP1B, the lytic transglycosylase MltA, and the scaffolding protein MipA of Escherichia coli

Vollmer, Waldemar, von Rechenberg, Moritz and Holtje, Joachim-Volker (1999). Demonstration of molecular interactions between the murein polymerase PBP1B, the lytic transglycosylase MltA, and the scaffolding protein MipA of Escherichia coli. Journal of Biological Chemistry, 274 (10), 6726-6734. doi: 10.1074/jbc.274.10.6726

Demonstration of molecular interactions between the murein polymerase PBP1B, the lytic transglycosylase MltA, and the scaffolding protein MipA of Escherichia coli

1998

Book Chapter

Growth of the bacterial sacculus requires both polymerization and depolymerization of murein

Höltje, J.V., Schiffer, G., Vollmer, W. and von Rechenberg, M. (1998). Growth of the bacterial sacculus requires both polymerization and depolymerization of murein. Biochemical principles and mechanisms of biosynthesis and biodegradation of polymers. (pp. 68-76) edited by A. Steinbüchel. Münster, Germany: Wiley.

Growth of the bacterial sacculus requires both polymerization and depolymerization of murein

1997

Journal Article

Outer membrane localization of murein hydrolases: MltA, a third lipoprotein lytic transglycosylase in Escherichia coli

Lommatzsch, J., Templin, M. F., Kraft, A. R., Vollmer, W. and Holtje, J. V. (1997). Outer membrane localization of murein hydrolases: MltA, a third lipoprotein lytic transglycosylase in Escherichia coli. Journal of Bacteriology, 179 (17), 5465-5470. doi: 10.1128/jb.179.17.5465-5470.1997

Outer membrane localization of murein hydrolases: MltA, a third lipoprotein lytic transglycosylase in Escherichia coli

1997

Journal Article

Pesticin displays muramidase activity

Vollmer, W., Pilsl, H., Hantke, K., Holtje, J. V. and Braun, V. (1997). Pesticin displays muramidase activity. Journal of Bacteriology, 179 (5), 1580-1583. doi: 10.1128/jb.179.5.1580-1583.1997

Pesticin displays muramidase activity

1993

Journal Article

Characterization of three different lytic transglycosylases in Escherichia coli

Romeis, Tina, Vollmer, Waldemar and Höltje, Joachim-Volker (1993). Characterization of three different lytic transglycosylases in Escherichia coli. FEMS Microbiology Letters, 111 (2-3), 141-146. doi: 10.1111/j.1574-6968.1993.tb06376.x

Characterization of three different lytic transglycosylases in Escherichia coli

Supervision

Availability

Professor Waldemar Vollmer is:
Available for supervision

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Supervision history

Current supervision

  • Doctor Philosophy

    Dissecting the bacterial cell envelope for antibiotic drug discovery

    Principal Advisor

    Other advisors: Dr Nicholas Ariotti, Professor Rob Capon

  • Doctor Philosophy

    Targeting bacterial cell envelope coordination for antibiotic drug discovery

    Principal Advisor

    Other advisors: Professor Brett Collins

  • Doctor Philosophy

    Novel assays for antibiotic discovery

    Principal Advisor

    Other advisors: Professor Rob Capon

Media

Enquiries

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