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Single molecule force spectroscopy reveals two-domain binding mode of pilus-1 tip protein RrgA of $Streptococcus\ pneumoniae$ to fibronectin
- Source :
- ACS Nano, ACS Nano, 2018, 12 (1), pp.549-558. ⟨10.1021/acsnano.7b07247⟩, ACS Nano, American Chemical Society, 2018, 12 (1), pp.549-558. ⟨10.1021/acsnano.7b07247⟩
- Publication Year :
- 2018
- Publisher :
- HAL CCSD, 2018.
-
Abstract
- International audience; For host cell adhesion and invasion, surface piliation procures benefits for bacteria. A detailed investigation of how pili adhere to host cells is therefore a key aspect inunderstanding their role during infection. Streptococcus pneumoniae TIGR 4, a clinical relevant serotype 4 strain, is capable of expressing pilus-1 with terminal RrgA, an adhesin interacting with host extracellular matrix (ECM) proteins. We used single molecule force spectroscopy to investigate the binding of full-length RrgA and single RrgA domains to fibronectin. Our results show that full-length RrgA and its terminal domains D3 and D4 bind to fibronectin with forces of 51.6 (full length), 52.8 (D3), and 46.2 pN (D4) at force-loading rates of around 1500 pN/s. Selective saturation of D3 and D4 binding sites on fibronectin showed that both domains can interact simultaneously with fibronectin, revealing a two-domain binding mechanism for the pilus-1 tip protein. The high off rates and the corresponding short lifetime of the RrgA Fn bond (τ = 0.26 s) may enable piliated pneumococci to form and maintain a transient contact to fibronectin-containing host surfaces and thus to efficiently scan the surface for specific receptors promoting host cell adhesion and invasion. These molecular properties could be essential for S. pneumoniae pili to mediate initial contact to the host cells andshared with other piliated Gram-positive bacteria_favor host invasion
- Subjects :
- 0301 basic medicine
Virulence Factors
General Physics and Astronomy
Microscopy, Atomic Force
Pneumococcal Infections
Pilus
Extracellular matrix
03 medical and health sciences
Protein Domains
fibronectin
Humans
General Materials Science
RrgA
Binding site
single molecule force spectroscopy
Binding Sites
biology
Strain (chemistry)
Chemistry
General Engineering
Force spectroscopy
Adhesion
Gram-positive bacteria
[SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology
Fibronectins
3. Good health
Cell biology
Fibronectin
Bacterial adhesin
030104 developmental biology
Streptococcus pneumoniae
Fimbriae, Bacterial
biology.protein
pili
Fimbriae Proteins
AFM
Protein Binding
Subjects
Details
- Language :
- English
- ISSN :
- 19360851
- Database :
- OpenAIRE
- Journal :
- ACS Nano, ACS Nano, 2018, 12 (1), pp.549-558. ⟨10.1021/acsnano.7b07247⟩, ACS Nano, American Chemical Society, 2018, 12 (1), pp.549-558. ⟨10.1021/acsnano.7b07247⟩
- Accession number :
- edsair.doi.dedup.....8ab9ce550f916d8b951192ac624ac7e9