The structure of Lactobacillus brevis surface layer reassembled on liposomes differs from native structure as revealed by SAXS |
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Authors: | Inkeri Kontro,Susanne K. Wiedmer,Ulla Hynö nen,Paavo A. Penttilä ,Airi Palva,Ritva Serimaa |
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Affiliation: | 1. Department of Physics, P.O.B. 64, 00014 University of Helsinki, Finland;2. Department of Chemistry, P.O.B. 55, 00014 University of Helsinki, Finland;3. Department of Veterinary Biosciences, P.O.B. 66, 00014 University of Helsinki, Finland |
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Abstract: | The reassembly of the S-layer protein SlpA of Lactobacillus brevis ATCC 8287 on positively charged liposomes was studied by small angle X-ray scattering (SAXS) and zeta potential measurements. SlpA was reassembled on unilamellar liposomes consisting of 1-palmitoyl-2-oleyl-sn-glycero-3-phosphocholine and 1,2-dioleoyl-3-trimethylammonium-propane, prepared by extrusion through membranes with pore sizes of 50 nm and 100 nm. Similarly extruded samples without SlpA were used as a reference. The SlpA-containing samples showed clear diffraction peaks in their SAXS intensities. The lattice constants were calculated from the diffraction pattern and compared to those determined for SlpA on native cell wall fragments. Lattice constants for SlpA reassembled on liposomes (a = 9.29 nm, b = 8.03 nm, and γ = 84.9°) showed a marked change in the lattice constants b and γ when compared to those determined for SlpA on native cell wall fragments (a = 9.41 nm, b = 6.48 nm, and γ = 77.0°). The latter are in good agreement with values previously determined by electron microscopy. This indicates that the structure formed by SlpA is stable on the bacterial cell wall, but SlpA reassembles into a different structure on cationic liposomes. From the (10) reflection, the lower limit of crystallite size of SlpA on liposomes was determined to be 92 nm, corresponding to approximately ten aligned lattice planes. |
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Keywords: | SAXS Liposomes S-layer Lactobacillus brevis |
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