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Identification of the hydroxyapatite-binding domain of salivary agglutinin.
MedLine Citation:
PMID:  23331418     Owner:  NLM     Status:  In-Data-Review    
Abstract/OtherAbstract:
The salivary agglutinin glycoprotein (SAG) is present in saliva but is also part of the salivary pellicle, playing a seemingly paradoxical role with regard to bacterial homeostasis. On the one hand, SAG aggregates bacteria in solution, thereby preventing bacterial colonization. On the other hand, when bound to the tooth surface, SAG facilitates bacterial colonization and microbial growth. The protein part of SAG is predominantly composed of conserved scavenger receptor cysteine-rich (SRCR) domains. Previously it was found that bacterial binding and aggregation is mediated via a single peptide loop, designated SRCRP2 (P2), within the SRCR domains of SAG. The current data suggest that the SRCR domains also harbour a hydroxyapatite (HA)-binding moiety, SRCRP3 (P3). The observation that P2 and P3 individually play unique roles in the function of SAGs contributes to our understanding of the dual role of SAGs in bacterial binding. Inspired by the bacterial-modulating capacity of SAGs, we created a P3-polyethylene glycol (PEG) conjugate. It was found that a P3 coating resulted in an increased antifouling activity of 20% compared with the uncoated surface in vitro. An additional PEG moiety resulted in an antifouling activity of up to 40% and 30% for Streptococcus mutans and Staphylococcus epidermidis, respectively.
Authors:
Floris J Bikker; Nivedita Cukkemane; Kamran Nazmi; Enno C I Veerman
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  European journal of oral sciences     Volume:  121     ISSN:  1600-0722     ISO Abbreviation:  Eur. J. Oral Sci.     Publication Date:  2013 Feb 
Date Detail:
Created Date:  2013-01-21     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9504563     Medline TA:  Eur J Oral Sci     Country:  England    
Other Details:
Languages:  eng     Pagination:  7-12     Citation Subset:  D; IM    
Copyright Information:
© 2013 Academic Centre for Dentistry Amsterdam, University of Amsterdam and VU University Amsterdam.
Affiliation:
Department of Oral Biochemistry, Academic Centre for Dentistry Amsterdam, University of Amsterdam, VU University Amsterdam, the Netherlands.
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