Neutron diffraction study of Pseudomonas aeruginosa lipopolysaccharide bilayers.
نویسندگان
چکیده
Lipopolysaccharides (LPSs) are a major class of macromolecules populating the surface of Gram-negative bacteria. They contribute significantly to the bacterium's surface properties and play a crucial role in regulating the permeability of its outer membrane. Here, we report on neutron diffraction studies performed on aligned, self-assembled bilayers of LPS isolated from Pseudomonas aeruginosa PAO1. This LPS system is comprised of a mixture of rough and smooth A-band and B-band LPS, similar to that naturally found in P. aeruginosa. Temperature scans were conducted at various levels of hydration, and the phases adopted by LPS, along with their corresponding transition temperatures, have been identified. Because of LPS's chemical heterogeneity, the gel-to-liquid-crystalline transition was continuous and not abrupt as commonly observed in single-component phospholipid systems. From the construction of one-dimensional scattering length density profiles, we find that water penetrates into the hydrocarbon region up to and including the center of liquid-crystalline LPS bilayers. This permeability to water also extends to bilayers in the continuous phase transition region and could have far-reaching implications as to how small molecules penetrate the outer membrane of Gram-negative bacteria.
منابع مشابه
Effect of cations on the structure of bilayers formed by lipopolysaccharides isolated from Pseudomonas aeruginosa PAO1.
The asymmetric outer membrane of Gram-negative bacteria contains lipopolysaccharides (LPSs) which contribute significantly to the bacterium's surface properties and play a crucial role in regulating membrane permeability. We report on neutron diffraction studies performed on aligned, self-assembled bilayers of Na-, Ca-, and Mg-salt forms of LPS isolated from Pseudomonas aeruginosa PAO1. From th...
متن کاملLipopolysaccharide-free Escherichia coli OmpF and Pseudomonas aeruginosa protein P porins are functionally active in lipid bilayer membranes.
Escherichia coli porin OmpF and Pseudomonas aeruginosa porin protein P were eluted from sodium dodecyl sulfate-polyacrylamide gels. The resultant porin preparations were found to be devoid of detectable lipopolysaccharide (LPS) by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and silver staining for LPS, direct enzyme-linked immunosorbent assays with LPS-specific monoclonal antibodi...
متن کاملDistribution of porin and lipopolysaccharide antigens on a Pseudomonas aeruginosa permeability mutant.
Pseudomonas aeruginosa common surface antigens were compared in a permeability mutant (PCC118) and its parent (PAO503). The distribution of lipopolysaccharide and porin antigens in the mutant supports the conclusion that beta-lactam permeability was affected by lipopolysaccharide-side chain presentation rather than by a change in porin number.
متن کاملInteraction of substance P with phospholipid bilayers: A neutron diffraction study.
Neutron diffraction has been used to study the membrane-bound structure of substance P (SP), a member of the tachykinin family of neuropeptides. The depth of penetration of its C-terminus in zwitterionic and anionic phospholipid bilayers was probed by specific deuteration of leucine 10, the penultimate amino acid residue. The results show that the interaction of SP with bilayers, composed of ei...
متن کاملAnion transport through the phosphate-specific OprP-channel of the Pseudomonas aeruginosa outer membrane: effects of phosphate, di- and tribasic anions and of negatively-charged lipids.
The mechanism of anion transport through the phosphate-starvation inducible OprP-channel of Pseudomonas aeruginosa outer membrane was studied in planar lipid bilayer membranes. The single-channel conductance of OprP was 160 pS in 100 mM chloride solution. Addition of other anions, in particular of phosphate, di and tribasic anions lead to a strong decrease of the chloride conductance. The decre...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- The journal of physical chemistry. B
دوره 111 10 شماره
صفحات -
تاریخ انتشار 2007