Craig D. Ellermeier, PhD


Associate Professor of Microbiology

Contact Information

Office: 3-630 Bowen Science Building
51 Newton Rd
Iowa City, IA 52242
Phone: 319-384-4565

Lab: 3-615C Bowen Science Building
51 Newton Rd
Iowa City, IA 52242
Phone: 319-335-7622

Email: craig-ellermeier@uiowa.edu


BS, Microbiology, Iowa State University
MS, Microbiology, University of Illinois at Urbana-Champaign
PhD, Microbiology, University of Illinois at Urbana-Champaign

Post Doctorate, Harvard University

Education/Training Program Affiliations

Department of Microbiology Graduate Program
Interdisciplinary Graduate Program in Genetics
Medical Scientist Training Program

Research Summary

Work in the Ellermeier Lab focuses on how two Gram positive bacteria, the model organism Bacillus subtilis and the opportunistic human pathogen Clostridium difficile, sense and respond to extracellular signals. We are particularly interested in understanding the response of C. difficile to factors produced by the innate immune system. We are interested in understanding how cells respond to changes in their environment by altering gene expression. To alter gene expression bacteria must detect changes in their environment and then transduce that signal from outside the cell to a transcriptional response inside the cell. We are interested in understanding the basic molecular mechanisms involved in how cells sense and respond to extracellular signals. We utilize genetic, molecular, biochemical and structural approaches to dissect these signal transduction systems.

Our work has revealed the presence of an Extra Cytoplasmic Function (ECF) σ factor, σV, present in B. subtilis and C. difficile that is activated specifically by lysozyme, an essential component of the innate immune system. We have found that σV is required for lysozyme resistance in both organisms. We have also found that σV is required for C. difficile to cause disease in an animal model of infection. The activity of σV is inhibited by the anti-sigma factor RsiV. Activation of σV occurs via proteolytic destruction of an anti-sigma factor RsiV. This degradation occurs only in the presence of lysozyme and requires multiple proteases to destroy RsiV in a process of regulated intramembrane proteolysis (RIP). We are interested in identifying the proteases required for σV activation and understanding the mechanism by which site-1 cleavage of RsiV, and thus σV activation, is controlled. We are also studying the role of additional ECF sigma factors encoded by C. difficile to determine their role in response to cell envelope stress. In addition we are interested in understanding the role of these ECF sigma factors play in survival of the bacterium during an infection.

A second area of focus for the laboratory is the process of cannibalism which occurs during B. subtilis sporulation. We are interested in understanding both the mechanisms of toxin production and how the senses and responds to the toxin SDP. Sporulation is initiated by the activation of a response regulator, Spo0A. The activity of Spo0A is not uniform across all cells of the population, in fact two subpopulations of B. subtilis exist, Spo0A-ON cells and Spo0A-OFF cells. The Spo0A-ON cells produce a toxin, SdpC, which is secreted and kills the SpoOA-OFF siblings. Normally, the Spo0A-ON cells resist the toxic effects of SDP by producing a membrane protein, SdpI, which provides immunity to the toxin. The immunity protein is only produced when extracellular toxin is present. Interestingly, SdpI is also required to induce its own expression in response to extracellular toxin sequestering a transcriptional repressor, SdpR, to the membrane. The sequestration of SdpR by the SdpC/SdpI complex inhibits the activity of the repressor thereby allowing increased transcription of sdpI, and immunity to the toxin.

Selected Publications

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Ho T, Ellermeier C.  Ferric Uptake Regulator Fur Control of Putative Iron Acquisition Systems in Clostridium difficile.  J Bacteriol.  2015 September. 197(18):2930-40.

Ransom E, Ellermeier C, Weiss D.  Use of mCherry Red fluorescent protein for studies of protein localization and gene expression in Clostridium difficile.  Appl Environ Microbiol.  2015 March. 81(5):1652-60.

Hastie J, Williams K, Sepúlveda C, Houtman J, Forest K, Ellermeier C.  Evidence of a bacterial receptor for lysozyme: binding of lysozyme to the anti-σ factor RsiV controls activation of the ecf σ factor σV.  PLoS Genet.  2014 October 2. 10(10):e1004643.

Ransom E, Williams K, Weiss D, Ellermeier C.  Identification and characterization of a gene cluster required for proper rod shape, cell division, and pathogenesis in Clostridium difficile.  J Bacteriol.  2014 June 15. 196(12):2290-2300.

Ho T, Williams K, Chen Y, Helm R, Popham D, Ellermeier C.  Clostridium difficile extracytoplasmic function σ factor σV regulates lysozyme resistance and is necessary for pathogenesis in the hamster model of infection.  Infect Immun.  2014 June. 82(6):2345-55.

Pérez Morales T, Ho T, Liu W, Dorrestein P, Ellermeier C.  Production of the cannibalism toxin SDP is a multistep process that requires SdpA and SdpB.  J Bacteriol.  2013 July. 195(14):3244-51.

Hastie J, Williams K, Ellermeier C.  The activity of σV, an extracytoplasmic function σ factor of Bacillus subtilis, is controlled by regulated proteolysis of the anti-σ factor RsiV.  J Bacteriol.  2013 July. 195(14):3135-44.

Ho T, Ellermeier C.  Extra cytoplasmic function σ factor activation.  Curr Opin Microbiol.  2012 April. 15(2):182-8.

Ho T, Hastie J, Intile P, Ellermeier C.  The Bacillus subtilis extracytoplasmic function σ factor σ(V) is induced by lysozyme and provides resistance to lysozyme.  J Bacteriol.  2011 November. 193(22):6215-22.

Ho T, Ellermeier C.  PrsW is required for colonization, resistance to antimicrobial peptides, and expression of extracytoplasmic function σ factors in Clostridium difficile.  Infect Immun.  2011 August. 79(8):3229-38.

Date Last Modified: 06/06/2016 - 13:17:48