Andrew Lee Lovering, Ph.D., School of Biosciences, University of Birmingham, has received a 2012 ICAAC Young Investigator Award for his seminal work on the structural biology and biochemistry of the proteins that synthesize and modify cell walls in bacteria. Natalie Strynadka, University of British Columbia, describes the significance of Lovering's work: "his spectacular abilities in structural biology clearly paved the way for our understanding of these important antibacterial targets which are also membrane-anchored, a hurdle that has thwarted literally decades of attempts at previous characterization by many groups worldwide." "His protein structure work has shown how Gram positive bacteria synthesize teichoic acids, how bacterial cell walls are transglycosylated, and how enzymes of predatory bacteria partially degrade bacterial cell walls as they invade prey bacteria," explained nominator Liz Sockett, University of Nottingham.
Lovering obtained his B.Sc. in Biochemistry from Birmingham University, where he also earned his Ph.D. in Biosciences. There he used x-ray crystallography to detail the mechanism of action of two enzymes involved in cancer therapies; one a bacterial nitroreductase used in gene therapy of solid tumors, and the other a target for a cell differentiation approach tackling acute myeloid leukemia.
After graduating from Birmingham University, a postdoctoral position in Strynadka's laboratory at the University of British Columbia introduced Lovering to the subject of antibacterial research. This led to determination of the structures of two monotopic membrane proteins involved in bacterial cell wall synthesis. One of these, S. aureus PBP2, represented the first detailed view of how bacteria catalyze the essential step of peptidoglycan polymerisation, a potentially excellent drug target. The other, S. epidermidis TagF, revealed how the Gram-positive wall polymer teichoic acid is synthesized and may form the basis for the development of antivirulents. The PBP2 publication was chosen as one of the highlights of the year by Science and C&E News.
Since establishing his own research group in 2010, Lovering's focus has shifted to deciphering the molecular basis of bacterial predation by Bdellovibrio bacteriovorus, a phenomenon that may lead to its exploitation as a "living antibiotic". In collaboration with Sockett at the University of Nottingham, this approach has already begun to detail how the invading bacterium modifies the prey cell wall for purposes of niche formation, and also how Bdellovibrio and other bacteria hydrolyze the ubiquitous bacterial second messenger cyclic-di-GMP. "As invited speaker of the 2012 Gordon Conference on Bacterial Sensory Transduction, he described the first ever crystal structure of an HD-GYP bacterial signaling protein," says Sockett.
"Lovering's enthusiasm and fascination with the microbial world is always palpable. His level of insight, profound knowledge of fundamental biochemistry, and ability to see connections that others would have missed never fail to amaze me," summarizes Klaus Ftterer, University of Birmingham. "As he builds his research group it is clear that his work will enlighten our understanding of an unusual microorganism, and his enthusiasm will inspire junior researchers in both the structural biology and microbiology communities."
Strynadka agrees, "he is highly collegial, modest, and a natural teacher. His love of and interest in science is truly infectiousknowledge he loves to share with others. Collectively, I believe him to be a truly exceptional rising star who will continue to make fundamental advances to structural microbiology."
|Contact: Garth Hogan|
American Society for Microbiology