Faculty

Matthew Chapman

Associate Professor of Molecular, Cellular, and Developmental Biology

Ph.D. Microbiology, Indiana University
B.S., Microbiology, University of Nebraska at Omaha

Research Focus: Amyloid biology and bacterial biofilm formation

Phone: 734.764.7592
E-mail: chapmanm@umich.edu

Our research is aimed at understanding the dynamic process that allows bacteria to integrate and adapt to their environment. The approach we’ve taken to this problem is to better understand the tools that microorganisms use to interact with themselves and their surroundings. This has led us to pursue extracellular organelle biology with special emphasis on curli fiber biogenesis by E. coli. During the course of our studies, we found that curli share distinguishing features with the medically important pathogenic amyloid fibers that are the hallmark of many neurodegenerative diseases such as Alzheimer’s, Huntington’s, systemic amyloidosis and the prion diseases.


Protein Misfolding Done Right

The discovery of a natural amyloid protein in E. coli opens up the possibility of performing genetic and biochemical experiments that are impractical or impossible in other amyloid model systems. Our work focuses on three related questions: how curli are assembled on the cell surface, how curli modify community behavior in bacteria, and how curli expression affects the host-pathogen interaction during an infection. We blend microscopy, biochemistry, and genetics in a concerted effort to delineate the structural, functional, and molecular details of curli, a distinct class of bacterial fibers that share properties with amyloid proteins. The curli biogenesis apparatus is possibly the world’s most tractable model system for understanding amyloid formation. But more than that, teasing apart the details of curli biogenesis will give insights into such fundamental bacterial processes as gene regulation, protein secretion and protein folding.


Curli Biogenesis

Much of the Chapman lab is interested in figuring out how curli amyloid fibers are assembled on the cell surface. Aggregation-prone curli subunits must be chaperoned from the inside of the cell to the outside, where they polymerize into stable amyloid fibers.


Biology of the Bacterial Extracellular Matrix

Cells in a biofilm are surrounded by an extracellular matrix that protects them from various stresses ranging from antibiotics to the host immune response. Resistance conferred by the extracellular matrix makes biofilm infections difficult to eradicate. Our lab is actively investigating the molecular pathways that control the extracellular matrix components, along with the role of the individual matrix components in biofilm resistance.


Protein Economics

Dan Smith was a graduate student in the lab who was interested in the evolutionary pressures on proteins.

Evolution is often thought of in functional terms. Mutations that improve or diversify a protein’s function are selected for, whereas disruptive mutations are selected against. However, economy can also play a role in protein evolution. Read all about it in Dan’s really cool paper: Economical Evolution: Microbes Reduce the Synthetic Cost of Extracellular Proteins



Chapman Research Group

 

Awards

2009 Class of 1923 Memorial Teaching Award from the University of Michigan
2004-2006 NIH Career Development Award K22
2001-2003 NIH Post-doctoral Fellowship F32

 

Representative Publications

  1. Hufnagel DA, Evans ML, Greene SE, Pinkner JS, Hultgren SJ and Chapman MR (2016) CRP-cAMP regulates csgD and biofilm formation by uropathogenic Escherichia coli J. Bacteriol. Accepted for publication.

  2. Horowitz S, Koepnick B, Martin R, Tymieniecki A, Winburn AA, Cooper S, Flatten J, Rogawski DS, Koropatkin NM, Hailu TT, Jain N, Koldewey P, Ahlstrom LS, Chapman MR et al. and Bardwell JC (2016). Determining crystal structures through crowdsourcing and coursework. Nat Commun. 7, 12549.

  3. Cremers CM, Knoefler D, Gates S, Martin N, Dahl JU, Lempart J, Xie L, Chapman MR, Galvan V, Southworth DR et al. and Jakob U (2016). Polyphosphate: A Conserved Modifier of Amyloidogenic Processes. Mol Cell. 63, 768-780.

  4. Floyd KA, Mitchell C, Eberly AR, Colling S, Zhang EW, DePas W, Chapman MR, Conover M, Rogers BR, Hultgren SJ and Hadjifrangiskou M (2016). The UbiI (VisC) aerobic ubiquinone synthase is required for expression of type 1 pili, biofilm formation, and pathogenesis in uropathogenic Escherichia coli. J. Bacteriology. In press.

  5. Taylor JD, Hawthorne WJ, Lo J, Dear A, Jain N, Meisl G, Andreasen M, Fletcher C, Koch M, Darvill N, Scull N, Escalera-Maurer A, Sefer L, Wenman R, Lambert S, Jean J, Xu Y, Turner B, Kazarian SG, Chapman MR, Bubeck D, de Simone A, Knowles TP, Matthews SJ (2016) Electrostatically-guided inhibition of Curli amyloid nucleation by the CsgC-like family of chaperones. Sci Rep, 6: 24656

  6. Hufnagel DA, Depas WH, Chapman MR (2015) The Biology of the Escherichia coli Extracellular Matrix. Microbiol Spectr, 3: PMID: 26185090

 

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