Document Detail

Polymorphisms in fibronectin binding protein A of Staphylococcus aureus are associated with infection of cardiovascular devices.
MedLine Citation:
PMID:  22025727     Owner:  NLM     Status:  MEDLINE    
Medical implants, like cardiovascular devices, improve the quality of life for countless individuals but may become infected with bacteria like Staphylococcus aureus. Such infections take the form of a biofilm, a structured community of bacterial cells adherent to the surface of a solid substrate. Every biofilm begins with an attractive force or bond between bacterium and substratum. We used atomic force microscopy to probe experimentally forces between a fibronectin-coated surface (i.e., proxy for an implanted cardiac device) and fibronectin-binding receptors on the surface of individual living bacteria from each of 80 clinical isolates of S. aureus. These isolates originated from humans with infected cardiac devices (CDI; n = 26), uninfected cardiac devices (n = 20), and the anterior nares of asymptomatic subjects (n = 34). CDI isolates exhibited a distinct binding-force signature and had specific single amino acid polymorphisms in fibronectin-binding protein A corresponding to E652D, H782Q, and K786N. In silico molecular dynamics simulations demonstrate that residues D652, Q782, and N786 in fibronectin-binding protein A form extra hydrogen bonds with fibronectin, complementing the higher binding force and energy measured by atomic force microscopy for the CDI isolates. This study is significant, because it links pathogenic bacteria biofilms from the length scale of bonds acting across a nanometer-scale space to the clinical presentation of disease at the human dimension.
Steven K Lower; Supaporn Lamlertthon; Nadia N Casillas-Ituarte; Roberto D Lins; Ruchirej Yongsunthon; Eric S Taylor; Alex C DiBartola; Catherine Edmonson; Lauren M McIntyre; L Barth Reller; Yok-Ai Que; Robert Ros; Brian H Lower; Vance G Fowler
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2011-10-24
Journal Detail:
Title:  Proceedings of the National Academy of Sciences of the United States of America     Volume:  108     ISSN:  1091-6490     ISO Abbreviation:  Proc. Natl. Acad. Sci. U.S.A.     Publication Date:  2011 Nov 
Date Detail:
Created Date:  2011-11-09     Completed Date:  2012-01-25     Revised Date:  2013-06-27    
Medline Journal Info:
Nlm Unique ID:  7505876     Medline TA:  Proc Natl Acad Sci U S A     Country:  United States    
Other Details:
Languages:  eng     Pagination:  18372-7     Citation Subset:  IM    
Ohio State University, Columbus, OH 43210, USA.
Data Bank Information
Bank Name/Acc. No.:
GENBANK/JF809617;  JF809618;  JF809619;  JF809620;  JF809621;  JF809622;  JF809623;  JF809624;  JF809625;  JF809626;  JF809627;  JF809628;  JF809629;  JF809630;  JF809631;  JF809632;  JF809633;  JF809634;  JF809635;  JF809636;  JF809637;  JF809638;  JF809639;  JF809640;  JF809641;  JF809642;  JF809643;  JF809644;  JF809645;  JF809646;  JF809647;  JF809648;  JF809649;  JF809650;  JF809651;  JF809652;  JF809653;  JF809654;  JF809655;  JF809656;  JF809657;  JF809658;  JF809659;  JF809660;  JF809661;  JF809662;  JN848717;  JN848718;  JN848719;  JN848720;  JN848721;  JN848722;  JN848723;  JN848724;  JN848725;  JN848726;  JN848727;  JN848728;  JN848729;  JN848730;  JN848731;  JN848732;  JN848733;  JN848734;  JN848735;  JN848736;  JN848737;  JN848738;  JN848739;  JN848740;  JN848741;  JN848742;  JN848743;  JN848744;  JN848745;  JN848746;  JN848747;  JN848748;  JN848749;  JN848750
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MeSH Terms
Adhesins, Bacterial / chemistry,  genetics*
Amino Acid Sequence
Amino Acid Substitution
Microscopy, Atomic Force
Molecular Dynamics Simulation
Molecular Sequence Data
Pacemaker, Artificial / microbiology*
Polymorphism, Genetic*
Sequence Homology, Amino Acid
Staphylococcus aureus / metabolism*
Grant Support
Reg. No./Substance:
0/Adhesins, Bacterial; 0/fibronectin-binding proteins, bacterial

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