Abstract
Bacteria associate with surfaces and one another by elaborating an extracellular matrix to encapsulate cells, creating communities termed biofilms. Biofilms are beneficial in some ecological niches, but also contribute to the pathogenesis of serious and chronic infectious diseases. New approaches and quantitative measurements are needed to define the composition and architecture of bacterial biofilms to help drive the development of strategies to interfere with biofilm assembly. Solid-state NMR is uniquely suited to the examination of insoluble and complex macromolecular and whole-cell systems. This article highlights three examples that implement solid-state NMR to deliver insights into bacterial biofilm composition and changes in cell-wall composition as cells transition to the biofilm lifestyle. Most recently, solid-state NMR measurements provided a total accounting of the protein and polysaccharide components in the extracellular matrix of an E. coli biofilm and transform our qualitative descriptions of matrix composition into chemical parameters that permit quantitative comparisons among samples. We present additional data for whole biofilm samples (cells plus the extracellular matrix) that complement matrix-only analyses. The study of bacterial biofilms by solid-state NMR is an exciting avenue ripe with many opportunities and we close the article by articulating some outstanding questions and future directions in this area.
PMID: 24976646 [PubMed - as supplied by publisher]
Solid-State NMR on Bacterial Cells: Selective Cell Wall Signal Enhancement and Resolution Improvement using Dynamic Nuclear Polarization
From the The DNP-NMR Blog:
Solid-State NMR on Bacterial Cells: Selective Cell Wall Signal Enhancement and Resolution Improvement using Dynamic Nuclear Polarization
Takahashi, H., et al., Solid-State NMR on Bacterial Cells: Selective Cell Wall Signal Enhancement and Resolution Improvement using Dynamic Nuclear Polarization. J. Am. Chem. Soc., 2013.
http://dx.doi.org/10.1021/ja312501d
Dynamic nuclear polarization (DNP) enhanced solid-state nuclear magnetic resonance (NMR) has recently emerged as a powerful technique for the study of material surfaces. In this study, we demonstrate...
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04-15-2013 08:52 AM
[NMR paper] Structure and orientation of bovine lactoferrampin in the mimetic bacterial membrane as revealed by solid-state NMR and molecular dynamics simulation.
Structure and orientation of bovine lactoferrampin in the mimetic bacterial membrane as revealed by solid-state NMR and molecular dynamics simulation.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif Related Articles Structure and orientation of bovine lactoferrampin in the mimetic bacterial membrane as revealed by solid-state NMR and molecular dynamics simulation.
Biophys J. 2012 Oct 17;103(8):1735-43
Authors: Tsutsumi A, Javkhlantugs N, Kira A, Umeyama M, Kawamura I, Nishimura K, Ueda K,...
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03-21-2013 02:58 PM
Revealing Protein Structures in Solid-Phase Peptide Synthesis by 13C Solid-State NMR: Evidence of Excessive Misfolding for Alzheimer’s ?
Revealing Protein Structures in Solid-Phase Peptide Synthesis by 13C Solid-State NMR: Evidence of Excessive Misfolding for Alzheimer’s ?
Songlin Wang and Yoshitaka Ishii
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja212190z/aop/images/medium/ja-2011-12190z_0002.gif
Journal of the American Chemical Society
DOI: 10.1021/ja212190z
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/6EE7uthrnLg
[NMR paper] Solid-state NMR studies of the membrane-bound closed state of the colicin E1 channel
Solid-state NMR studies of the membrane-bound closed state of the colicin E1 channel domain in lipid bilayers.
Related Articles Solid-state NMR studies of the membrane-bound closed state of the colicin E1 channel domain in lipid bilayers.
Protein Sci. 1998 Feb;7(2):342-8
Authors: Kim Y, Valentine K, Opella SJ, Schendel SL, Cramer WA
The colicin E1 channel polypeptide was shown to be organized anisotropically in membranes by solid-state NMR analysis of samples of uniformly 15N-labeled protein in oriented planar phospholipid bilayers. The 190...
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11-17-2010 11:06 PM
[NMR paper] Solid-state REDOR NMR distance measurements at the ligand site of a bacterial chemota
Solid-state REDOR NMR distance measurements at the ligand site of a bacterial chemotaxis membrane receptor.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Solid-state REDOR NMR distance measurements at the ligand site of a bacterial chemotaxis membrane receptor.
Biochemistry. 1997 Feb 18;36(7):1699-703
Authors: Wang J, Balazs YS, Thompson LK
The Escherichia coli serine receptor senses serine levels in the environment and transmits this information across the bacterial inner membrane to...
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08-22-2010 03:31 PM
[NMR paper] Solid-state REDOR NMR distance measurements at the ligand site of a bacterial chemota
Solid-state REDOR NMR distance measurements at the ligand site of a bacterial chemotaxis membrane receptor.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Solid-state REDOR NMR distance measurements at the ligand site of a bacterial chemotaxis membrane receptor.
Biochemistry. 1997 Feb 18;36(7):1699-703
Authors: Wang J, Balazs YS, Thompson LK
The Escherichia coli serine receptor senses serine levels in the environment and transmits this information across the bacterial inner membrane to...
Solid-State NMR for Bacterial Biofilms.
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