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

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• 作者：Wenxing Tang ; Avni Bhatt ; Adam N. Smith ; Paula J. Crowley…
• 关键词：Gram ; positive bacteria ; Streptococcus mutans ; Dental caries ; Adhesin ; Amyloid ; Cell surface ; Solid ; state NMR
• 刊名：Journal of Biomolecular NMR
• 出版年：2016
• 出版时间：February 2016
• 年：2016
• 卷：64
• 期：2
• 页码：153-164
• 全文大小：2,612 KB
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• 作者单位：Wenxing Tang (1) (2)
  Avni Bhatt (1)
  Adam N. Smith (3)
  Paula J. Crowley (2)
  L. Jeannine Brady (2)
  Joanna R. Long (1)
  
  1. Department of Biochemistry and Molecular Biology, College of Medicine, University of Florida, Gainesville, FL, USA
  2. Department of Oral Biology, College of Dentistry, University of Florida, Gainesville, FL, USA
  3. Department of Chemistry, College of Liberal Arts and Sciences, University of Florida, Gainesville, FL, USA
  
• 刊物类别：Physics and Astronomy
• 刊物主题：Physics
  Biophysics and Biomedical Physics
  Polymer Sciences
  Biochemistry
  
• 出版者：Springer Netherlands
• ISSN：1573-5001

文摘

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