Show simple item record

Bonds between fibronectin and fibronectin-binding proteins on Staphylococcus aureus and Lactococcus lactis.

dc.contributor.author Buck, AW
dc.contributor.author DiBartola, AC
dc.contributor.author Fowler, Vance Garrison Jr
dc.contributor.author Liu, J
dc.contributor.author Lower, SK
dc.contributor.author Moreillon, P
dc.contributor.author Que, YA
dc.contributor.author Yongsunthon, R
dc.coverage.spatial United States
dc.date.accessioned 2011-06-21T17:26:58Z
dc.date.issued 2010-07-06
dc.identifier http://www.ncbi.nlm.nih.gov/pubmed/20218549
dc.identifier.uri http://hdl.handle.net/10161/4085
dc.description.abstract Bacterial cell-wall-associated fibronectin binding proteins A and B (FnBPA and FnBPB) form bonds with host fibronectin. This binding reaction is often the initial step in prosthetic device infections. Atomic force microscopy was used to evaluate binding interactions between a fibronectin-coated probe and laboratory-derived Staphylococcus aureus that are (i) defective in both FnBPA and FnBPB (fnbA fnbB double mutant, DU5883), (ii) capable of expressing only FnBPA (fnbA fnbB double mutant complemented with pFNBA4), or (iii) capable of expressing only FnBPB (fnbA fnbB double mutant complemented with pFNBB4). These experiments were repeated using Lactococcus lactis constructs expressing fnbA and fnbB genes from S. aureus. A distinct force signature was observed for those bacteria that expressed FnBPA or FnBPB. Analysis of this force signature with the biomechanical wormlike chain model suggests that parallel bonds form between fibronectin and FnBPs on a bacterium. The strength and covalence of bonds were evaluated via nonlinear regression of force profiles. Binding events were more frequent (p < 0.01) for S. aureus expressing FnBPA or FnBPB than for the S. aureus double mutant. The binding force, frequency, and profile were similar between the FnBPA and FnBPB expressing strains of S. aureus. The absence of both FnBPs from the surface of S. aureus removed its ability to form a detectable bond with fibronectin. By contrast, ectopic expression of FnBPA or FnBPB on the surface of L. lactis conferred fibronectin binding characteristics similar to those of S. aureus. These measurements demonstrate that fibronectin-binding adhesins FnBPA and FnBPB are necessary and sufficient for the binding of S. aureus to prosthetic devices that are coated with host fibronectin.
dc.language eng
dc.language.iso en_US
dc.relation.ispartof Langmuir
dc.relation.isversionof 10.1021/la100549u
dc.relation.isreplacedby 10161/13322
dc.relation.isreplacedby http://hdl.handle.net/10161/13322
dc.subject Bacterial Proteins
dc.subject Biofilms
dc.subject Carrier Proteins
dc.subject Fibronectins
dc.subject Lactococcus lactis
dc.subject Staphylococcus aureus
dc.title Bonds between fibronectin and fibronectin-binding proteins on Staphylococcus aureus and Lactococcus lactis.
dc.title.alternative
dc.type Journal article
dc.description.version Version of Record
duke.date.pubdate 2010-7-6
duke.description.issue 13
duke.description.volume 26
dc.relation.journal Langmuir
pubs.author-url http://www.ncbi.nlm.nih.gov/pubmed/20218549
pubs.begin-page 10764
pubs.end-page 10770
pubs.issue 13
pubs.organisational-group Basic Science Departments
pubs.organisational-group Clinical Science Departments
pubs.organisational-group Duke
pubs.organisational-group Duke Clinical Research Institute
pubs.organisational-group Institutes and Centers
pubs.organisational-group Medicine
pubs.organisational-group Medicine, Infectious Diseases
pubs.organisational-group Molecular Genetics and Microbiology
pubs.organisational-group School of Medicine
pubs.publication-status Published
pubs.volume 26
dc.identifier.eissn 1520-5827


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record