Document Detail


The role of ionic interactions in the adherence of the Staphylococcus epidermidis adhesin SdrF to prosthetic material.
MedLine Citation:
PMID:  23039791     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Staphylococcus epidermidis infections are common complications of prosthetic device implantation. SdrF, a surface protein, appears to play a critical role in the initial colonization step by adhering to type I collagen and Dacron™. The role of ionic interactions in S. epidermidis adherence to prosthetic material was examined. SdrF was cloned and expressed in Lactococcus lactis. The effect of pH, cation concentration, and detergents on adherence to different types of plastic surfaces was assessed by crystal violet staining and bacterial cell counting. SdrF, in contrast with controls and other S. epidermidis surface proteins, bound to hydrophobic materials such as polystyrene. Binding was an ionic interaction and was affected by surface charge of the plastic, pH, and cation concentration. Adherence of the SdrF construct was increased to positively charged plastics and was reduced by increasing concentrations of Ca(2+) and Na(+). Binding was optimal at pH 7.4. Kinetic studies demonstrated that the SdrF B domain as well as one of the B subdomains was sufficient to mediate binding. The SdrF construct also bound more avidly to Goretex™ than the lacotococcal control. SdrF is a multifunctional protein that contributes to prosthetic devices infections by ionic, as well as specific receptor-ligand interactions.
Authors:
Faustino A Toba; Livia Visai; Sheetal Trivedi; Franklin D Lowy
Publication Detail:
Type:  Letter; Research Support, N.I.H., Extramural     Date:  2012-11-02
Journal Detail:
Title:  FEMS microbiology letters     Volume:  338     ISSN:  1574-6968     ISO Abbreviation:  FEMS Microbiol. Lett.     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2012-12-12     Completed Date:  2013-06-12     Revised Date:  2014-01-10    
Medline Journal Info:
Nlm Unique ID:  7705721     Medline TA:  FEMS Microbiol Lett     Country:  England    
Other Details:
Languages:  eng     Pagination:  24-30     Citation Subset:  IM    
Copyright Information:
© 2012 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved.
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MeSH Terms
Descriptor/Qualifier:
Adhesins, Bacterial / metabolism*
Bacterial Adhesion*
Bacterial Proteins / metabolism
Humans
Ions / metabolism*,  pharmacology
Kinetics
Membrane Proteins / metabolism
Plastics
Polystyrenes
Prostheses and Implants / microbiology*
Staphylococcus epidermidis / physiology*
Grant Support
ID/Acronym/Agency:
HL 077096-01/HL/NHLBI NIH HHS; P50 HL077096/HL/NHLBI NIH HHS
Chemical
Reg. No./Substance:
0/Adhesins, Bacterial; 0/Bacterial Proteins; 0/Ions; 0/Membrane Proteins; 0/Plastics; 0/Polystyrenes
Comments/Corrections

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