[NMR paper] Specific binding of a naturally occurring amyloidogenic fragment of Streptococcus mutans adhesin P1 to intact P1 on the cell surface characterized by solid state NMR spectroscopy.
Specific binding of a naturally occurring amyloidogenic fragment of Streptococcus mutans adhesin P1 to intact P1 on the cell surface characterized by solid state NMR spectroscopy.
Specific binding of a naturally occurring amyloidogenic fragment of Streptococcus mutans adhesin P1 to intact P1 on the cell surface characterized by solid state NMR spectroscopy.
J Biomol NMR. 2016 Feb 2;
Authors: Tang W, Bhatt A, Smith AN, Crowley PJ, Brady LJ, Long JR
Abstract
The P1 adhesin (aka Antigen I/II or PAc) of the cariogenic bacterium Streptococcus mutans is a cell surface-localized protein involved in sucrose-independent adhesion and colonization of the tooth surface. The immunoreactive and adhesive properties of S. mutans suggest an unusual functional quaternary ultrastructure comprised of intact P1 covalently attached to the cell wall and interacting with non-covalently associated proteolytic fragments thereof, particularly the ~57-kDa C-terminal fragment C123 previously identified as Antigen II. S. mutans is capable of amyloid formation when grown in a biofilm and P1 is among its amyloidogenic proteins. The C123 fragment of P1 readily forms amyloid fibers in vitro suggesting it may play a role in the formation of functional amyloid during biofilm development. Using wild-type and P1-deficient strains of S. mutans, we demonstrate that solid state NMR (ssNMR) spectroscopy can be used to (1) globally characterize cell walls isolated from a Gram-positive bacterium and (2) characterize the specific binding of heterologously expressed, isotopically-enriched C123 to cell wall-anchored P1. Our results lay the groundwork for future high-resolution characterization of the C123/P1 ultrastructure and subsequent steps in biofilm formation via ssNMR spectroscopy, and they support an emerging model of S. mutans colonization whereby quaternary P1-C123 interactions confer adhesive properties important to binding to immobilized human salivary agglutinin.
PMID: 26837620 [PubMed - as supplied by publisher]
Specific binding of a naturally occurring amyloidogenic fragment of Streptococcus mutans adhesin P1 to intact P1 on the cell surface characterized by solid state NMR spectroscopy
Specific binding of a naturally occurring amyloidogenic fragment of Streptococcus mutans adhesin P1 to intact P1 on the cell surface characterized by solid state NMR spectroscopy
Abstract
The P1 adhesin (aka Antigen I/II or PAc) of the cariogenic bacterium Streptococcus mutans is a cell surface-localized protein involved in sucrose-independent adhesion and colonization of the tooth surface. The immunoreactive and adhesive properties of S. mutans suggest an unusual functional quaternary ultrastructure comprised of intact P1 covalently attached to the...
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02-02-2016 08:58 PM
[NMR paper] Insight into the Supramolecular Architecture of Intact Diatom Biosilica from DNP-Supported Solid-State NMR Spectroscopy.
Insight into the Supramolecular Architecture of Intact Diatom Biosilica from DNP-Supported Solid-State NMR Spectroscopy.
Related Articles Insight into the Supramolecular Architecture of Intact Diatom Biosilica from DNP-Supported Solid-State NMR Spectroscopy.
Angew Chem Int Ed Engl. 2015 Oct 28;
Authors: Jantschke A, Koers E, Mance D, Weingarth M, Brunner E, Baldus M
Abstract
Diatom biosilica is an inorganic/organic hybrid with interesting properties. The molecular architecture of the organic material at the atomic and nanometer...
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10-29-2015 10:08 PM
Polymorphs of Theophylline Characterized by DNP Enhanced Solid-State NMR
From The DNP-NMR Blog:
Polymorphs of Theophylline Characterized by DNP Enhanced Solid-State NMR
Pinon, A.C., et al., Polymorphs of Theophylline Characterized by DNP Enhanced Solid-State NMR. Mol Pharm, 2015.
http://www.ncbi.nlm.nih.gov/pubmed/26393368
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10-28-2015 05:05 PM
Revealing Cell-Surface Intramolecular Interactionsin the BlaR1 Protein of Methicillin-Resistant Staphylococcusaureus by NMR Spectroscopy
Revealing Cell-Surface Intramolecular Interactionsin the BlaR1 Protein of Methicillin-Resistant Staphylococcusaureus by NMR Spectroscopy
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi401552j/aop/images/medium/bi-2013-01552j_0003.gif
Biochemistry
DOI: 10.1021/bi401552j
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
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12-25-2013 02:06 AM
[NMR paper] Solid-state NMR in the analysis of drugs and naturally occurring materials.
Solid-state NMR in the analysis of drugs and naturally occurring materials.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Solid-state NMR in the analysis of drugs and naturally occurring materials.
J Pharm Biomed Anal. 2013 Oct 14;
Authors: Paradowska K, Wawer I
Abstract
This article presents some of the solid-state NMR (SSNMR) techniques used in the pharmaceutical and biomedical research. Solid-state magic angle spinning (MAS) NMR provides...
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11-01-2013 07:39 PM
Quantitation of Recombinant Protein in Whole Cellsand Cell Extracts via Solid-State NMR Spectroscopy
Quantitation of Recombinant Protein in Whole Cellsand Cell Extracts via Solid-State NMR Spectroscopy
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi4007034/aop/images/medium/bi-2013-007034_0004.gif
Biochemistry
DOI: 10.1021/bi4007034
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06-17-2013 06:41 PM
[NMR paper] Quantitation of Recombinant Protein in Whole Cells and Cell Extracts with Solid-State NMR Spectroscopy.
Quantitation of Recombinant Protein in Whole Cells and Cell Extracts with Solid-State NMR Spectroscopy.
Related Articles Quantitation of Recombinant Protein in Whole Cells and Cell Extracts with Solid-State NMR Spectroscopy.
Biochemistry. 2013 Jun 6;
Authors: Vogel EP, Weliky DP
Abstract
Recombinant proteins (RPs) are commonly expressed in bacteria followed by solubilization and chromatography. Purified RP yield can be diminished by losses at any step with very different changes in methods needed to try to improve yield. Time and...
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06-08-2013 02:18 PM
Naturally occurring biodegradable polymers as the basis of chiral gels for the distinction of enantiomers by partially oriented NMR spectroscopy.
Naturally occurring biodegradable polymers as the basis of chiral gels for the distinction of enantiomers by partially oriented NMR spectroscopy.
Naturally occurring biodegradable polymers as the basis of chiral gels for the distinction of enantiomers by partially oriented NMR spectroscopy.
Int J Artif Organs. 2011 Feb;34(2):134-8
Authors: Büchler SS, Kummerlöwe G, Luy B
In modern, high resolution NMR spectroscopy, anisotropic parameters play an important role. They can be measured with the help of liquid crystalline mesophases or stretched...