Reciprocal influence between the protein and lipid components of a lipid-protein membrane model

Diederich, Anke; Sponer, C.; Pum, Dietmar; Sleytr, Uwe B.; Lösche, Mathias

doi:10.1016/0927-7765(96)01267-2

Cited by 68 publications

(60 citation statements)

References 30 publications

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“…Fourier-transform infrared spectroscopy revealed an altered phase transition behavior of the lipid membrane ( Fig. 2), which is in qualitative accordance with the findings described for other non-specific S-layer-phospholipid assemblies (Diederich et al, 1996;Küpcü et al, 1998). The quantitative effects and functional implications for outer membranes await investigation.…”

Section: S-layer-outer Membrane Associationssupporting

confidence: 71%

“…Similar to the expected situation in Grampositive bacteria, the S-layer has an impact on the physico-chemical characteristics of the underlying cell envelope component. Although experimental data on natural systems are rare (Gerbl-Rieger et al, 1992), measurements with artificial S-layer-membrane (phospholipid) assemblies indicate possible effects (Diederich et al, 1996;Hirn et al, 1999;Küpcü et al, 1998;Mader et al, 1999;Schuster et al, 1998Schuster et al, , 1999Schuster and Sleytr, 2002;Sleytr et al, 2001). Here, S-layers from Gram-positive bacteria were recrystallised on homogeneous lipid monolayers or bilayers.…”

Section: S-layer-outer Membrane Associationsmentioning

confidence: 99%

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Are S-layers exoskeletons? The basic function of protein surface layers revisited

Engelhardt

2007

Journal of Structural Biology

137

121

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Surface protein or glycoprotein layers (Slayers) are common structures of the prokaryotic cell envelope. They are either associated with the peptidoglycan or outer membrane of bacteria, and constitute the only cell wall component of many archaea. Despite their occurrence in most of the phylogenetic branches of microorganisms, the functional significance of S-layers is assumed to be specific for genera or groups of organisms in the same environment rather than common to all prokaryotes. Functional aspects have usually been investigated with isolated S-layer sheets or proteins, which disregards the interactions between S-layers and the underlying cell envelope components. This study discusses the synergistic effects in cell envelope assemblies, the hypothetical role of S-layers for cell shape formation, and the existence of a common function in view of new insights.

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Section: S-layer-outer Membrane Associationssupporting

confidence: 71%

Section: S-layer-outer Membrane Associationsmentioning

confidence: 99%

Are S-layers exoskeletons? The basic function of protein surface layers revisited

Engelhardt

2007

Journal of Structural Biology

137

121

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“…This accumulation at domain edges implies that attractive forces are acting between Fn in the LE phase and the domains. The insertion of proteins into the LE phase and migration to domain boundaries is not unique to Fn and has been observed for several other proteins (21,(23)(24)(25). Two nonexclusive theoretical models have been proposed to account for the attractive interaction between domain boundaries and surface-adsorbed proteins in the LE phase: attractive dipole͞dipole interactions (26) and entropy-driven depletion forces (27).…”

Section: Resultsmentioning

confidence: 99%

Self-assembly of fibronectin into fibrillar networks underneath dipalmitoyl phosphatidylcholine monolayers: Role of lipid matrix and tensile forces

Baneyx

Vogel

1999

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

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The cell-mediated assembly of fibronectin (Fn) into fibrillar matrices is a complex multistep process that is incompletely understood because of the chemical complexity of the extracellular matrix and a lack of experimental control over molecular interactions and dynamic events. We have identified conditions under which Fn assembles into extended fibrillar networks after adsorption to a dipalmitoyl phosphatidylcholine (DPPC) monolayer in contact with physiological buffer. We propose a sequential model for the Fn assembly pathway, which involves the orientation of Fn underneath the lipid monolayer by insertion into the liquid expanded (LE) phase of DPPC. Attractive interactions between these surfaceanchored proteins and the liquid condensed (LC) domains leads to Fn enrichment at domain edges. Spontaneous self-assembly into fibrillar networks, however, occurs only after expansion of the DPPC monolayer from the LC phase though the LC͞LE phase coexistence. Upon monolayer expansion, the domain boundaries move apart while attractive interactions among Fn molecules and between Fn and domain edges produce a tensile force on the proteins that initiates fibril assembly. The resulting fibrils have been characterized in situ by using fluorescence and light-scattering microscopy. We have found striking similarities between fibrils produced under DPPC monolayers and those found on cellular surfaces, including their assembly pathways.

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“…Perhaps the first is whether these proteins will adsorb onto the monolayer and under which conditions. For instance, Diederich et al [105] used FTIR to show that the S-layer protein from Bacillus sphaericus CCM2177 does not interpenetrate but rather couples to the monolayer via lipid head groups. Polverine et al [106] showed with FTIR measurements that a myelin basic protein (MBP) binds to negatively charged phospholipids thus forming a complex.…”

Section: Cell Membrane Modelsmentioning

confidence: 99%

Vibrational spectroscopy for probing molecular-level interactions in organic films mimicking biointerfaces

Volpati

Aoki

Aléssio

et al. 2014

Advances in Colloid and Interface Science

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Reciprocal influence between the protein and lipid components of a lipid-protein membrane model

Cited by 68 publications

References 30 publications

Are S-layers exoskeletons? The basic function of protein surface layers revisited

Are S-layers exoskeletons? The basic function of protein surface layers revisited

Self-assembly of fibronectin into fibrillar networks underneath dipalmitoyl phosphatidylcholine monolayers: Role of lipid matrix and tensile forces

Vibrational spectroscopy for probing molecular-level interactions in organic films mimicking biointerfaces

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