scholarly journals Effect of Divalent Cation Removal on the Structure of Gram-Negative Bacterial Outer Membrane Models

Langmuir ◽  
2014 ◽  
Vol 31 (1) ◽  
pp. 404-412 ◽  
Author(s):  
Luke A. Clifton ◽  
Maximilian W. A. Skoda ◽  
Anton P. Le Brun ◽  
Filip Ciesielski ◽  
Ivan Kuzmenko ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Divalent Cation ◽  
Gram Negative ◽  
Bacterial Outer Membrane ◽  
Membrane Models

scholarly journals Dewetting-induced formation and mechanical properties of synthetic bacterial outer membrane models (GUVs) with controlled inner-leaflet lipid composition

Soft Matter ◽  
2019 ◽  
Vol 15 (19) ◽  
pp. 3938-3948 ◽  
Author(s):  
Sepehr Maktabi ◽  
Jeffrey W. Schertzer ◽  
Paul R. Chiarot
Keyword(s):  
Mechanical Properties ◽  
Outer Membrane ◽  
Lipid Composition ◽  
Membrane Lipid ◽  
Giant Unilamellar Vesicles ◽  
Gram Negative ◽  
Membrane Lipid Composition ◽  
Bacterial Outer Membrane ◽  
Membrane Models ◽  
Microfluidic Technique

We report on a microfluidic technique for fabricating monodisperse asymmetric giant unilamellar vesicles (GUVs) possessing the Gram-negative bacterial outer membrane lipid composition.

scholarly journals Asymmetric phospholipid: lipopolysaccharide bilayers; a Gram-negative bacterial outer membrane mimic

2013 ◽  
Vol 10 (89) ◽  
pp. 20130810 ◽  
Author(s):  
Luke A. Clifton ◽  
Maximilian W. A. Skoda ◽  
Emma L. Daulton ◽  
Arwel V. Hughes ◽  
Anton P. Le Brun ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Lipid A ◽  
Membrane Dynamics ◽  
Gram Negative ◽  
Outer Leaflet ◽  
Physical Study ◽  
Bacterial Outer Membrane ◽  
Membrane Models ◽  
Initial Deposition

The Gram-negative bacterial outer membrane (OM) is a complex and highly asymmetric biological barrier but the small size of bacteria has hindered advances in in vivo examination of membrane dynamics. Thus, model OMs, amenable to physical study, are important sources of data. Here, we present data from asymmetric bilayers which emulate the OM and are formed by a simple two-step approach. The bilayers were deposited on an SiO 2 surface by Langmuir–Blodgett deposition of phosphatidylcholine as the inner leaflet and, via Langmuir–Schaefer deposition, an outer leaflet of either Lipid A or Escherichia coli rough lipopolysaccharides (LPS). The membranes were examined using neutron reflectometry (NR) to examine the coverage and mixing of lipids between the bilayer leaflets. NR data showed that in all cases, the initial deposition asymmetry was mostly maintained for more than 16 h. This stability enabled the sizes of the headgroups and bilayer roughness of 1,2-dipalmitoyl- sn -glycero-3-phosphocholine and Lipid A, Rc-LPS and Ra-LPS to be clearly resolved. The results show that rough LPS can be manipulated like phospholipids and used to fabricate advanced asymmetric bacterial membrane models using well-known bilayer deposition techniques. Such models will enable OM dynamics and interactions to be studied under in vivo -like conditions.

scholarly journals Dynamic interaction of fluoroquinolones with magnesium ions monitored using bacterial outer membrane nanopores

2020 ◽  
Vol 11 (38) ◽  
pp. 10344-10353
Author(s):  
Jiajun Wang ◽  
Jigneshkumar Dahyabhai Prajapati ◽  
Ulrich Kleinekathöfer ◽  
Mathias Winterhalter
Keyword(s):  
Outer Membrane ◽  
Divalent Cations ◽  
Dynamic Interaction ◽  
Gram Negative Bacteria ◽  
Magnesium Ions ◽  
Gram Negative ◽  
Bacterial Outer Membrane

Divalent cations alter the translocation of antibiotic molecules through the Gram-negative bacteria outer membrane nanopores.

scholarly journals Mechanism of anchoring of OmpA protein to the cell wall peptidoglycan of the gram‐negative bacterial outer membrane

2011 ◽  
Vol 26 (1) ◽  
pp. 219-228 ◽  
Author(s):  
Jeong Soon Park ◽  
Woo Cheol Lee ◽  
Kwon Joo Yeo ◽  
Kyoung‐Seok Ryu ◽  
Malika Kumarasiri ◽  
...  
Keyword(s):  
Cell Wall ◽  
Outer Membrane ◽  
Gram Negative ◽  
Cell Wall Peptidoglycan ◽  
Ompa Protein ◽  
Bacterial Outer Membrane

Epitope mapping of monoclonal antibodies specific for the directly cross-linkedmeso-diaminopimelic acid peptidoglycan found in the anaerobic beer spoilage bacteriumPectinatus cerevisiiphilus

1999 ◽  
Vol 45 (9) ◽  
pp. 779-785 ◽  
Author(s):  
Barry Ziola ◽  
Sheryl L Gares ◽  
Brandene Lorrain ◽  
Lori Gee ◽  
W M Ingledew ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Outer Membrane ◽  
Epitope Mapping ◽  
Sodium Dodecyl ◽  
Diaminopimelic Acid ◽  
Gram Negative Bacteria ◽  
Gram Negative ◽  
Spoilage Bacteria ◽  
Beer Spoilage ◽  
Bacterial Outer Membrane

Nineteen monoclonal antibodies (Mabs) were isolated based on reactivity with disrupted Pectinatus cerevisiiphilus cells. All of the Mabs reacted with cells from which the outer membrane had been stripped by incubation with sodium dodecyl sulphate, suggesting the peptidoglycan (PG) layer was involved in binding. Mab reactivity with purified PG confirmed this. Epitope mapping revealed the Mabs in total recognize four binding sites on the PG. Mabs specific for each of the four sites also bound strongly to disrupted Pectinatus frisingensis, Selenomonas lacticifix, Zymophilus paucivorans, and Zymophilus raffinosivorans cells, but weakly to disrupted Megasphaera cerevisiae cells. No antibody reactivity was seen with disrupted cells of 11 other species of Gram-negative bacteria. These results confirm that a common PG structure is used by several species of anaerobic Gram-negative beer spoilage bacteria. These results also indicate that PG-specific Mabs can be used to rapidly detect a range of anaerobic Gram-negative beer spoilage bacteria, provided the bacterial outer membrane is first removed to allow antibody binding.Key words: beer spoilage, epitope mapping, monoclonal antibodies, Pectinatus, peptidoglycan.

Proteomics in gram-negative bacterial outer membrane vesicles

2008 ◽  
Vol 27 (6) ◽  
pp. 535-555 ◽  
Author(s):  
Eun-Young Lee ◽  
Dong-Sic Choi ◽  
Kwang-Pyo Kim ◽  
Yong Song Gho
Keyword(s):  
Outer Membrane ◽  
Membrane Vesicles ◽  
Outer Membrane Vesicles ◽  
Gram Negative ◽  
Bacterial Outer Membrane
Sign in / Sign up

Export Citation Format

Share Document