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Structure of the bacterial cell division determinant GpsB and its interaction with penicillin binding proteins

DOI: 10.1111/mmi.13279 DOI Help
PMID: 26575090 PMID Help

Authors: Jeanine Rismondo (Robert Koch Institute) , Robert Cleverley (Newcastle University) , Harriet Lane (University of Newcastle) , Stephanie Großhennig (Robert Koch Institute) , Anne Steglich (Robert Koch Institute) , Lars Möller (University of Gießen) , Gopala Krishna Mannala (University of Gießen) , Torsten Hain (University of Gießen) , Richard J. Lewis (University of Newcastle) , Sven Halbedel (Robert Koch Institute)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Molecular Microbiology

State: Published (Approved)
Published: November 2015

Abstract: Each bacterium has to co-ordinate its growth with division to ensure genetic stability of the population. Consequently, cell division and growth are tightly-regulated phenomena, albeit different bacteria utilise one of several alternative regulatory mechanisms to maintain control. Here we consider GpsB, which is linked to cell growth and division in Gram-positive bacteria. ΔgpsB mutants of the human pathogen Listeria monocytogenes show severe lysis, division and growth defects due to distortions of cell wall biosynthesis. Consistent with this premise, GpsB interacts both in vitro and in vivo with the major bi-functional penicillin binding protein. We solved the crystal structure of GpsB and the interaction interfaces in both proteins are identified and validated. The inactivation of gpsB results in strongly attenuated virulence in animal experiments, comparable in degree to classical listerial virulence factor mutants. Therefore, GpsB is essential for in vitro and in vivo growth of a highly virulent food-borne pathogen, suggesting that GpsB could be a target for the future design of novel antibacterials.

Subject Areas: Biology and Bio-materials


Instruments: I04-Macromolecular Crystallography

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