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Surface layer proteins

Johnson-Henry, K. C., Hagen, K. E., Gordonpour, M., Tompkins, T. A., and Sherman, P. M. (2007). Surface-layer protein extracts from Lactobacillus helveticus inhibit entero-haemorrhagic Escherichia coli 0157 H7 adhesion to epithelial cells. Cell. Microbiol. 9, 356-367. [Pg.149]

Peters, J., Baumeister, W., and Lupas, A. (1996). Hyperthermostable surface layer protein tetrabrachion from the archaebacterium Staphylothermus marinusr. Evidence for the presence of a right-handed coiled coil derived from the primary structure. / Mol. Biol. 257, 1031-1041. [Pg.76]

Fig. 3. Monitoring of the variant formation in a continuous culture of Bacillus stearothermo-philus PV72 (as in Fig. 2) by SDS-PAGE. The organisms differed in the S- (surface) layer proteins. The wild type formed an S-layer protein of 130 kDa apparent molecular mass, the variant S-layer protein appears at 97 kDa molecular mass. The wild-type S-layer protein was quantified relative to the band of the altered protein by densitometry. Numbers on the curve represent samples harvested at distinct points of time during variant formation. The decrease of the wild-type S-layer protein followed the theoretical washout curve in a stirred tank reactor at the set dilution rate of 0.3 h 1 (Reprinted from J. Biotechnol. 54, K. C. Schuster et al, p. 20,1997, with permission from Elsevier Science)... Fig. 3. Monitoring of the variant formation in a continuous culture of Bacillus stearothermo-philus PV72 (as in Fig. 2) by SDS-PAGE. The organisms differed in the S- (surface) layer proteins. The wild type formed an S-layer protein of 130 kDa apparent molecular mass, the variant S-layer protein appears at 97 kDa molecular mass. The wild-type S-layer protein was quantified relative to the band of the altered protein by densitometry. Numbers on the curve represent samples harvested at distinct points of time during variant formation. The decrease of the wild-type S-layer protein followed the theoretical washout curve in a stirred tank reactor at the set dilution rate of 0.3 h 1 (Reprinted from J. Biotechnol. 54, K. C. Schuster et al, p. 20,1997, with permission from Elsevier Science)...
Jing H, Takagi J, Liu JH ct al. Archaeal surface layer proteins contain beta propeller, PKD and beta helix domains and are related to metazoan cell surface proteins. Structiuc 2002 10(10) 1453-64. [Pg.29]

Biotemplates have been fabricated from two-dimensional crystalline surface proteins for the subsequent electrochemical deposition of nanowire structures [82]. These surface layer proteins encapsulate certain bacterial cells, controlling extracellular transport. They form especially robust thin films over cells, and are resistant to conditions that normally denature proteins, such as low pH and heat, thus making them ideal as template materials for electrodeposition. Schwartz and coworkers investigated a hexagonally packed intermediate surface layer protein from... [Pg.203]

Deinococcu radiodurans, with 2-3 nm pores and widths of 5-6 mn (Fig. 13.11). The surface layer proteins were bound to the cells by hydrophobic interactions and were extracted using a detergent, sodium dodecyl sulfate (SDS). The resulting templates have been randomly dispersed on conductive substrates for through-mask deposition of Cu O, Ni, Pt, Pd, and Co [82]. [Pg.205]

Surface layer proteins (S-layers) represent a unique self-assembling system. Their remarkable property of self-assembUng and their repetitive physicochemical properties, down to the nanometer scale, are promising for various applications. [Pg.57]

Messner, P., 1996. Chemical composition and bios3Tithesis of S-layers. In Sleytr, U.B., Messner, P., Pum, D., Sara, M. (Eds.), Crystalline Bacterial Cell Surface Layer Proteins (S-layers). Academic Press, Landes Company, Austin, TX, pp. 35—76. [Pg.89]

Schaffer, C., Messner, P., 2001. Glycobiology of surface layer proteins. Biochemistry 83, 591-599. [Pg.90]

Chapter 3, Self-assembly of nanobiomaterials, prepared by Varga et al., offers a recent review regarding the surface-layer proteins (S-layers) that represent a unique self-assembling system. Their remarkable property of self-assembling and their repetitive physicochemical properties down to the nanometer scale led to various applications in the fields of bio- and nanotechnology. Chapter 3 focuses on the basic principles and self-assembly properties of the S-layer protein of Sporosarcina ureae. [Pg.511]

Discrimination of Microbial Strains Based on Typing of Flagellin and Surface Layer Proteins... [Pg.130]

Cell envelopes in numerous bacteria and archaea are covered by a porous layer of proteins. Moreover, for the majority of bacteria this proteinaceous surface layer is de facto composed from numerous identical protein subunits with in the range of 25-200 kDa, and with a copy numbers exceeding 5 x 10 subunits (Sleytr and Messner 1983), thus making them an attractive target for extraction (see Section Surface Layer Proteins ) and sequence-based discrimination of microbial strains. [Pg.133]

Hynonen U, Palva A. Lactobacillus surface layer proteins structure, function and applications. Appl Microbiol Biotechnol. 2013 97 5225 3. doi 10.1007/s00253-013 962-2. [Pg.141]

Podlesny M, Jarocki P, Komon E, et al. LC-MS/MS analysis of surface layer proteins as a useful method for the identification of lactobacilli from the Lactobacillus acidophilus group. J Microbiol Biotechnol. 2011 21 421 9. doi 10.4014/jmb.l009.09036. [Pg.144]

As shown by Pockels, Langmuir [24 - 26] and others, amphiphilic molecules, including lipids, can be stabilised as monomolecular layers at the air-water interface. Also, some proteins can self-assemble - on their own or with lipids - at the air-water interface to form monolayers, e.g., lipase [27], bacterial surface-layer proteins [28, 29], or trans-membrane proteins such as bacteriorhodopsin [30], Transfer of monomolecular layers to solid support by the Langmuir-... [Pg.206]

The structural model sketched in Figure 6 was based [28, 29] on the electron density profile and the available knowledge of the lipid, dipalmitoylphosphatidylethanolamine (DPPE) and of the surface layer protein from B. sphaericus CCM2177. [Pg.223]

Figure 6 Artist s view of lipid/protein interaction derived from the electron density model from XR measurements and available structural data. The lipid monolayer is dipalmitoyl phosphatidyl ethanolamine (DPPE) and the protein is a membrane surface layer protein from B. sphaericus (from ref. [28]). The structural model sketched was based [28, 29] on the electron density profile (black line) inverted from measured reflectivity data as described in the text. Figure 6 Artist s view of lipid/protein interaction derived from the electron density model from XR measurements and available structural data. The lipid monolayer is dipalmitoyl phosphatidyl ethanolamine (DPPE) and the protein is a membrane surface layer protein from B. sphaericus (from ref. [28]). The structural model sketched was based [28, 29] on the electron density profile (black line) inverted from measured reflectivity data as described in the text.
L. Peyret, N. Bayan, G. Joliff, T. Gulik-Krzywicki, L. Mathieu, E. Schechter, and G. Leblon, Characterization of the cspB gene encoding PS2, an ordered surface-layer protein in Corynebacterium glutamicum. Mol Microbiol, 9,97-109 (1993). [Pg.678]

Allred, D. B., A. Cheng, M. Sarikaya, F. Baneyx, and D. T. Schwartz. 2008. Three-dimensional architecture of inorganic nanoarrays electrodeposited through a surface-layer protein mask. Nano Letts. 8 1434-1438. [Pg.617]

Ultrasonics/ultrasound this is a new approach that requires further development (Zhou et fl/.,2002 Navot et a/., 2011). In one example, ultrasound has been evaluated to administer vaccines for the control of goldfish ulcer disease, which is caused by atypical A. sa/momc/da. Thus, soluble surface layer protein (= A-protein) of A. salmonicida was applied by immersion after ultrasound (1 MHz frequency of ultrasound/1 min) pretreatment, and led to promising results after challenge (Navot et al., 2011). [Pg.220]


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See also in sourсe #XX -- [ Pg.57 , Pg.63 , Pg.64 , Pg.65 , Pg.68 , Pg.74 ]




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