ArticleProceedings of the National Academy of Sciences of the United States of America2016
Zinc-dependent mechanical properties of Staphylococcus aureus biofilm-forming surface protein SasG.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.
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Who cites it
81 citing papers in PubMed, 161 citations in OpenAlex.
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- Comparison of the antibiotic resistance mechanisms in a gram-positive and a gram-negative bacterium by gene networks analysis.PloS one · 2024Article
- Comparative De Novo and Pan-Genome Analysis of MDR Nosocomial Bacteria Isolated from Hospitals in Jeddah, Saudi Arabia.Microorganisms · 2023Article
- Convergent behavior of extended stalk regions from staphylococcal surface proteins with widely divergent sequence patterns.Protein science : a publication of the Protein Society · 2023Article
- Comparative Analysis of Physical and Chemical Properties of Differently Obtained Zn-Methionine Chelate with Proved Antibiofilm Properties (Part II).Pharmaceutics · 2023Article
- Staphylococcus epidermidis and its dual lifestyle in skin health and infection.Nature reviews. Microbiology · 2023Review
- Convergent behavior of extended stalk regions from staphylococcal surface proteins with widely divergent sequence patterns.bioRxiv : the preprint server for biology · 2023Article
21 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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 Zn(2+) 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 Zn(2+)-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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