Nanoscale membrane architecture of healthy and pathological red blood cells

Dumitru, Andra C.; Poncin, Mégane A.; Conrard, Louise; Dufrêne, Yves F.; Tyteca, Donatienne; Alsteens, David

doi:10.1039/c7nh00187h

Cited by 46 publications

(44 citation statements)

References 57 publications

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“…5c, e), which is in the range of values reported for E. coli (0.04 N m −1 ) 25,26 and for the two other Gram-negative bacteria Shewanella putrefaciens (0.02-0.05 N m −1 ) 19 and Pseudomonas aeruginosa (0.02 N m −1 ) 27 . We note that similar trends were obtained using the FV and QI modes, the later yielding larger values, which we believe results from the much higher speed of QI 28 .…”

Section: Resultssupporting

confidence: 81%

Lipoprotein Lpp regulates the mechanical properties of the E. coli cell envelope

et al. 2020

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The mechanical properties of the cell envelope in Gram-negative bacteria are controlled by the peptidoglycan, the outer membrane, and the proteins interacting with both layers. In Escherichia coli, the lipoprotein Lpp provides the only covalent crosslink between the outer membrane and the peptidoglycan. Here, we use single-cell atomic force microscopy and genetically engineered strains to study the contribution of Lpp to cell envelope mechanics. We show that Lpp contributes to cell envelope stiffness in two ways: by covalently connecting the outer membrane to the peptidoglycan, and by controlling the width of the periplasmic space. Furthermore, mutations affecting Lpp function substantially increase bacterial susceptibility to the antibiotic vancomycin, indicating that Lpp-dependent effects can affect antibacterial drug efficacy.

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Section: Resultssupporting

confidence: 81%

Lipoprotein Lpp regulates the mechanical properties of the E. coli cell envelope

et al. 2020

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“…We can therefore not exclude the possibility that the Chol-enriched domain population that was not revealed by Laurdan exhibits a higher order than the bulk. Accordingly, high spatial resolution atomic force microscopy of the RBC membrane allowed us to reveal lipid domains correlated with both local minima and maxima areas in the Young's modulus maps [33]. This suggests that the RBC membrane is composed of lipid domains exhibiting differential local mechanical properties, which could depend on the specific lipid domain composition and on their differential association to membrane and cytoskeletal proteins.…”

Section: Discussionmentioning

confidence: 99%

“…Additionally, by mimicking RBC membrane vesiculation upon aging by storage at 4°C, we showed that both lipid domains represent specific sites for membrane vesiculation upon aging [31]. Fourth, we recently showed by high spatial resolution atomic force microscopy that the RBC membrane is composed of lipid domains exhibiting differential local mechanical properties, which could depend on their differential association to the cytoskeleton and on their specific lipid composition [33]. However, atomic force microscopy does not allow to determine the lipid composition of the domains nor to evaluate how their mechanical properties are modulated upon RBC deformation.…”

Section: Introductionmentioning

confidence: 99%

Tuning of Differential Lipid Order Between Submicrometric Domains and Surrounding Membrane Upon Erythrocyte Reshaping

Léonard

Pollet

Vermylen

et al. 2018

Cell Physiol Biochem

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Background/Aims: Transient nanometric cholesterol- and sphingolipid-enriched domains, called rafts, are characterized by higher lipid order as compared to surrounding lipids. Here, we asked whether the seminal concept of highly ordered rafts could be refined with the presence of lipid domains exhibiting different enrichment in cholesterol and sphingomyelin and association with erythrocyte curvature areas. We also investigated how differences in lipid order between domains and surrounding membrane (bulk) are regulated and whether changes in order differences could participate to erythrocyte deformation and vesiculation. Methods: We used the fluorescent hydration- and membrane packing-sensitive probe Laurdan to determine by imaging mode the Generalized Polarization (GP) values of lipid domains vs the surrounding membrane. Results: Laurdan revealed the majority of sphingomyelin-enriched domains associated to low erythrocyte curvature areas and part of the cholesterol-enriched domains associated with high curvature. Both lipid domains were less ordered than the surrounding lipids in erythrocytes at resting state. Upon erythrocyte deformation (elliptocytes and stimulation of calcium exchanges) or membrane vesiculation (storage at 4°C), lipid domains became more ordered than the bulk. Upon aging and in membrane fragility diseases (spherocytosis), an increase in the difference of lipid order between domains and the surrounding lipids contributed to the initiation of domain vesiculation. Conclusion: The critical role of domain-bulk differential lipid order modulation for erythrocyte reshaping is discussed in relation with the pressure exerted by the cytoskeleton on the membrane.

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“…More recently, we also used atomic force microscopy, a high-resolution technique applicable to cells in their native state (i.e. without labeling), to study the biophysical properties of these domains [28]. The chol-and SM-enriched domains differ in abundance and biophysical properties (i.e.…”

Section: Introductionmentioning

confidence: 99%

Spatial Relationship and Functional Relevance of Three Lipid Domain Populations at the Erythrocyte Surface

Conrard

Stommen

Cloos

et al. 2018

Cell Physiol Biochem

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Background/Aims: Red blood cells (RBC) have been shown to exhibit stable submicrometric lipid domains enriched in cholesterol (chol), sphingomyelin (SM), phosphatidylcholine (PC) or ganglioside GM1, which represent the four main lipid classes of their outer plasma membrane leaflet. However, whether those lipid domains co-exist at the RBC surface or are spatially related and whether and how they are subjected to reorganization upon RBC deformation are not known. Methods: Using fluorescence and/or confocal microscopy and well-validated probes, we compared these four lipid-enriched domains for their abundance, curvature association, lipid order, temperature dependence, spatial dissociation and sensitivity to RBC mechanical stimulation. Results: Our data suggest that three populations of lipid domains with decreasing abundance coexist at the RBC surface: (i) chol-enriched ones, associated with RBC high curvature areas; (ii) GM1/PC/chol-enriched ones, present in low curvature areas; and (iii) SM/PC/chol-enriched ones, also found in low curvature areas. Whereas chol-enriched domains gather in increased curvature areas upon RBC deformation, low curvature-associated lipid domains increase in abundance either upon calcium influx during RBC deformation (GM1/PC/chol-enriched domains) or upon secondary calcium efflux during RBC shape restoration (SM/PC/chol-enriched domains). Hence, abrogation of these two domain populations is accompanied by a strong impairment of the intracellular calcium balance. Conclusion: Lipid domains could contribute to calcium influx and efflux by controlling the membrane distribution and/or the activity of the mechano-activated ion channel Piezo1 and the calcium pump PMCA. Whether this results from lipid domain biophysical properties, the strength of their anchorage to the underlying cytoskeleton and/or their correspondence with inner plasma membrane leaflet lipids remains to be demonstrated.

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Nanoscale membrane architecture of healthy and pathological red blood cells

Abstract: Red blood cells present a complex cell plasma membrane architecture with submicrometric organization leading to nanomechanical heterogeneities.

Cited by 46 publications

References 57 publications

Lipoprotein Lpp regulates the mechanical properties of the E. coli cell envelope

Lipoprotein Lpp regulates the mechanical properties of the E. coli cell envelope

Tuning of Differential Lipid Order Between Submicrometric Domains and Surrounding Membrane Upon Erythrocyte Reshaping

Spatial Relationship and Functional Relevance of Three Lipid Domain Populations at the Erythrocyte Surface

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