Dissociation Rate Constants of Human Fibronectin Binding to Fibronectin-binding Proteins on Living Staphylococcus aureus Isolated from Clinical Patients

Casillas-Ituarte, Nadia N.; Lower, Brian H.; Lamlertthon, Supaporn; Fowler, Vance G.; Lower, Steven K.

doi:10.1074/jbc.m111.285692

Cited by 29 publications

(48 citation statements)

References 68 publications

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“…Together, the present study and other recent investigations (12,13,26) support the hypothesis that S. aureus endovascular syndromes are correlatable to amino acid polymorphisms and/or duplications within high-affinity Fn-binding regions of FnBPs. These changes in FnBPs may indeed lead to stronger binding reactions and enhanced capacity to initiate an infection (12).…”

Section: Fig 4 Qrt-pcr Of Fnbb the Effect Of Clonal Variation On Fnbsupporting

confidence: 72%

“…There were both similarities and differences between these FnBPA alterations and previously reported perturbations in S. aureus strains obtained from CDI patients (12,13,26). In terms of similarities, polymorphisms were observed in three high-affinity Fn-binding repeats (FnBR-9, -10, and -11) for our bacteremia isolates.…”

Section: Fig 4 Qrt-pcr Of Fnbb the Effect Of Clonal Variation On Fnbmentioning

confidence: 57%

“…For example, bacteremia isolates of S. aureus from U.S. patients with CDIs have signature, nonsynonymous SNPs in FnBPA (E652D, H782Q, and K786N) versus bacteremia isolates from patients with cardiac implants in place that are uninfected (CDU). In addition, the CDI isolates formed a more resilient bond with Fn, as determined by AFM and computational simulations (12,26). This link between CDI and polymorphisms in high-affinity Fn-binding repeats of FnBPA in the U.S. patient cohort has since been externally validated using an independent cohort of European S. aureus isolates (13).…”

Section: Discussionmentioning

confidence: 99%

“…The prevalence of the fnbB gene on these 10 isolates was determined by using standard PCR techniques as described above and the primer pair fnbB-F (5=-CTTTACCTTGTTCCACTGGTTTAGAAG-3=) and fnbB-R (5=-GGGAGTAACAGCTAATGGTCG-3=). The surface expression of FnBPs on all ten S. aureus isolates was confirmed by Western ligand blotting, as described previously (26).…”

Section: Methodsmentioning

confidence: 99%

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Endovascular Infections Caused by Methicillin-Resistant Staphylococcus aureus Are Linked to Clonal Complex-Specific Alterations in Binding and Invasion Domains of Fibronectin-Binding Protein A as Well as the Occurrence of fnbB

et al. 2015

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e Endovascular infections caused by Staphylococcus aureus involve interactions with fibronectin present as extracellular matrix or surface ligand on host cells. We examined the expression, structure, and binding activity of the two major S. aureus fibronectinbinding proteins (FnBPA, FnBPB) in 10 distinct, methicillin-resistant clinical isolates from patients with either persistent or resolving bacteremia. The persistent bacteremia isolates (n ‫؍‬ 5) formed significantly stronger bonds with immobilized fibronectin as determined by dynamic binding measurements performed with atomic force microscopy. Several notable differences were also observed when the results were grouped by clonal complex 5 (CC5) strains (n ‫؍‬ 5) versus CC45 strains (n ‫؍‬ 5). Fibronectinbinding receptors on CC5 formed stronger bonds with immobilized fibronectin (P < 0.001). The fnbA gene was expressed at higher levels in CC45, whereas fnbB was found in only CC5 isolates. The fnbB gene was not sequenced because all CC45 isolates lacked this gene. Instead, comparisons were made for fnbA, which was present in all 10 isolates. Sequencing of fnbA revealed discrete differences within high-affinity, fibronectin-binding repeats (FnBRs) of FnBPA that included (i) 5-amino-acid polymorphisms in FnBR-9, FnBR-10, and FnBR-11 involving charged or polar side chains, (ii) an extra, 38-amino-acid repeat inserted between FnBR-9 and FnBR-10 exclusively seen in CC45 isolates, and (iii) CC5 isolates had the SVDFEED epitope in FnBR-11 (a sequence shown to be essential for fibronectin binding), while this sequence was replaced in all CC45 isolates with GIDFVED (a motif known to favor host cell invasion at the cost of reduced fibronectin binding). These complementary sequence and binding data suggest that differences in fnbA and fnbB, particularly polymorphisms and duplications in FnBPA, give S. aureus two distinct advantages in human endovascular infections: (i) FnBPs similar to that of CC5 enhance ligand binding and foster initiation of disease, and (ii) CC45-like FnBPs promote cell invasion, a key attribute in persistent endovascular infections.

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Section: Fig 4 Qrt-pcr Of Fnbb the Effect Of Clonal Variation On Fnbsupporting

confidence: 72%

Section: Fig 4 Qrt-pcr Of Fnbb the Effect Of Clonal Variation On Fnbmentioning

confidence: 57%

Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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Endovascular Infections Caused by Methicillin-Resistant Staphylococcus aureus Are Linked to Clonal Complex-Specific Alterations in Binding and Invasion Domains of Fibronectin-Binding Protein A as Well as the Occurrence of fnbB

et al. 2015

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“…Recent advances in atomic force microscopy (AFM) techniques have enabled researchers to gain insight into the biophysical properties and molecular interactions of microbial cells (17,18), including S. aureus (19)(20)(21)(22). A variety of AFM-based force spectroscopy methods have been developed, in which the force acting on the AFM probe is measured with piconewton (10 −12 N) sensitivity as the probe is pushed toward the sample, then retracted from it (17).…”

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confidence: 99%

Zinc-dependent mechanical properties of Staphylococcus aureus biofilm-forming surface protein SasG

Formosa-Dague

Speziale

Foster

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

137

132

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Staphylococcus aureus surface protein SasG promotes cell–cell adhesion during the accumulation phase of biofilm formation, but the molecular basis of this interaction remains poorly understood. Here, we unravel the mechanical properties of SasG on the surface of living bacteria, that is, in its native cellular environment. Nanoscale multiparametric imaging of living bacteria reveals that Zn2+ strongly increases cell wall rigidity and activates the adhesive function of SasG. Single-cell force measurements show that SasG mediates cell–cell adhesion via specific Zn2+-dependent homophilic bonds between β-sheet–rich G5–E domains on neighboring cells. The force required to unfold individual domains is remarkably strong, up to ∼500 pN, thus explaining how SasG can withstand physiological shear forces. We also observe that SasG forms homophilic bonds with the structurally related accumulation-associated protein of Staphylococcus epidermidis, suggesting the possibility of multispecies biofilms during host colonization and infection. Collectively, our findings support a model in which zinc plays a dual role in activating cell–cell adhesion: adsorption of zinc ions to the bacterial cell surface increases cell wall cohesion and favors the projection of elongated SasG proteins away from the cell surface, thereby enabling zinc-dependent homophilic bonds between opposing cells. This work demonstrates an unexpected relationship between mechanics and adhesion in a staphylococcal surface protein, which may represent a general mechanism among bacterial pathogens for activating cell association.

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Probing ligand-receptor bonds in physiologically relevant conditions using AFM

2019

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Dissociation Rate Constants of Human Fibronectin Binding to Fibronectin-binding Proteins on Living Staphylococcus aureus Isolated from Clinical Patients

Cited by 29 publications

References 68 publications

Endovascular Infections Caused by Methicillin-Resistant Staphylococcus aureus Are Linked to Clonal Complex-Specific Alterations in Binding and Invasion Domains of Fibronectin-Binding Protein A as Well as the Occurrence of fnbB

Endovascular Infections Caused by Methicillin-Resistant Staphylococcus aureus Are Linked to Clonal Complex-Specific Alterations in Binding and Invasion Domains of Fibronectin-Binding Protein A as Well as the Occurrence of fnbB

Zinc-dependent mechanical properties of Staphylococcus aureus biofilm-forming surface protein SasG

Probing ligand-receptor bonds in physiologically relevant conditions using AFM

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