Journal of Biomolecular NMR

, Volume 64, Issue 2, pp 153–164 | Cite as

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

  • Wenxing Tang
  • Avni Bhatt
  • Adam N. Smith
  • Paula J. Crowley
  • L. Jeannine BradyEmail author
  • Joanna R. LongEmail author


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.


Gram-positive bacteria Streptococcus mutans Dental caries Adhesin Amyloid Cell surface Solid-state NMR 



Monoclonal antibody


Magic angle spinning


Nuclear magnetic resonance


Solid-state NMR


Congo red


Salivary agglutinin glycoprotein complex



We would like to thank Drs. Kyle Heim and Richard Besingi for helpful discussions. This work was supported in part by National Institutes of Health Grants R01DE08007 and R01DE21789 from the NIDCR. A portion of this work was performed in the McKnight Brain Institute at the National High Magnetic Field Laboratory’s AMRIS Facility, which is supported by National Science Foundation Cooperative Agreement No. DMR-1157490, the State of Florida, and an NIH award, S10RR031637, for magnetic resonance instrumentation.

Supplementary material

10858_2016_17_MOESM1_ESM.pdf (574 kb)
Supplementary material 1 (PDF 573 kb)


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Copyright information

© Springer Science+Business Media Dordrecht 2016

Authors and Affiliations

  • Wenxing Tang
    • 1
    • 2
  • Avni Bhatt
    • 1
  • Adam N. Smith
    • 3
  • Paula J. Crowley
    • 2
  • L. Jeannine Brady
    • 2
    Email author
  • Joanna R. Long
    • 1
    Email author
  1. 1.Department of Biochemistry and Molecular Biology, College of MedicineUniversity of FloridaGainesvilleUSA
  2. 2.Department of Oral Biology, College of DentistryUniversity of FloridaGainesvilleUSA
  3. 3.Department of Chemistry, College of Liberal Arts and SciencesUniversity of FloridaGainesvilleUSA

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