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Nanonewton forces between Staphylococcus aureus surface protein IsdB and vitronectin.

ABSTRACT: Single-molecule experiments have recently revealed that the interaction between staphylococcal surface proteins and their ligands can be extremely strong, equivalent to the strength of covalent bonds. Here, we report on the unusually high binding strength between Staphylococcus aureus iron-regulated surface determinant B (IsdB) and vitronectin (Vn), an essential human blood protein known to interact with bacterial pathogens. The IsdB-Vn interaction is dramatically strengthened by mechanical tension, with forces up to 2000 pN at a loading rate of 10⁵ pN s^-1. In line with this, flow experiments show that IsdB-mediated bacterial adhesion to Vn is enhanced by fluid shear stress. The stress-dependent binding of IsdB to Vn is likely to play a role in promoting bacterial adhesion to human cells under fluid shear stress conditions.

SUBMITTER: Mathelie-Guinlet M

PROVIDER: S-EPMC9419033 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature

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Nanonewton forces between <i>Staphylococcus aureus</i> surface protein IsdB and vitronectin.

Mathelié-Guinlet Marion M Viela Felipe F Pietrocola Giampiero G Speziale Pietro P Dufrêne Yves F YF

Nanoscale advances 20201030 12

Single-molecule experiments have recently revealed that the interaction between staphylococcal surface proteins and their ligands can be extremely strong, equivalent to the strength of covalent bonds. Here, we report on the unusually high binding strength between <i>Staphylococcus aureus</i> iron-regulated surface determinant B (IsdB) and vitronectin (Vn), an essential human blood protein known to interact with bacterial pathogens. The IsdB-Vn interaction is dramatically strengthened by mechanic ...[more]

PMID: 36133863

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Project description:Staphylococcus aureus is a well-recognized, clinically important cause of nosocomial infections, and as such, a vaccine to prevent S. aureus infections would be an important achievement. A Phase IIB/III study of V710, a vaccine containing iron-regulated surface determinant B (IsdB), demonstrated significant sero-conversion rates in cardiovascular surgery patients following a single pre-surgery immunization. However, the vaccine was not efficacious in preventing bacteremia or deep sternal wound infection post-surgery, thus raising the possibility that IsdB might not be available for immune recognition during infection. The purpose of the work described herein was to evaluate and quantify the naturally occurring anti-IsdB levels at baseline and over time during infection, to understand whether IsdB is expressed during a S. aureus infection in hospitalized non-vaccinated patients. We evaluated baseline and follow-up titers in 3 populations: (1) healthy subjects, (2) hospitalized patients with non-S. aureus infections, and (3) hospitalized patients with S. aureus infections. Baseline anti-IsdB levels generally overlapped between the 3 groups, but were highly variable within each group. In healthy subjects, baseline and follow-up levels were highly correlated (Spearman's rho = 0.93), and the geometric mean fold-rise (GMFR) in anti-IsdB levels between study entry and last value was 0.9-fold (95% confidence interval (CI): 0.8 to 1.0 ; p = 0.09), showing no trend over time. The convalescent GMFR in anti-IsdB levels from baseline was 1.7-fold (95% CI: 1.3 to 2.2, p = 0.0008) during S. aureus infection, significantly different from the 1.0-fold GMFR (95% CI: 0.9-1.2, p = 0.60) in non-S. aureus infection, p = 0.005. Additionally, S. aureus isolates (51) obtained from the hospitalized patient group expressed the IsdB protein in vitro. Collectively, these data suggest that IsdB expression levels rise substantially following infection with S. aureus, but not with other pathogens, and IsdB is likely well-conserved across S. aureus strains.

Dataset Information

Nanonewton forces between Staphylococcus aureus surface protein IsdB and vitronectin.

Publications

Nanonewton forces between <i>Staphylococcus aureus</i> surface protein IsdB and vitronectin.

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