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Relevance of glycosylation of S-layer proteins for cell surface properties.

Schuster B, Sleytr UB - Acta Biomater (2015)

Bottom Line: Interestingly, to the wtSgsE lattice almost twice the amount of water is bound and/or coupled in comparison with the non-glycosylated rSgsE with the preferred region being the extending glycan residues.The present results are discussed in terms of the effect of the glycan residues on the recrystallization, the adjoining hydration layer, and the nanoscale roughness and fluidic behavior.The latter features may turn out to be one of the most general ones among bacterial and archaeal S-layer lattices.

View Article: PubMed Central - PubMed

Affiliation: Institute for Synthetic Bioarchitectures, Department of NanoBiotechnology, University of Natural Resources and Life Sciences, Vienna, Muthgasse 11, 1190 Vienna, Austria. Electronic address: bernhard.schuster@boku.ac.at.

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Recrystallization process of two different S-layer (glyco)proteins from Geobacillus stearothermophilus NRS 2004/3a (protein concentration of 50 μg mL−1) on gold-covered sensor surfaces as followed by quartz crystal microbalance with dissipation monitoring (QCM-D). The shift in frequency (left axis) and dissipation (right axis) as a function of time at the 5th overtone is shown for (A) the S-layer glycoprotein wtSgsE and (B) for the S-layer protein rSgsE.
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f0020: Recrystallization process of two different S-layer (glyco)proteins from Geobacillus stearothermophilus NRS 2004/3a (protein concentration of 50 μg mL−1) on gold-covered sensor surfaces as followed by quartz crystal microbalance with dissipation monitoring (QCM-D). The shift in frequency (left axis) and dissipation (right axis) as a function of time at the 5th overtone is shown for (A) the S-layer glycoprotein wtSgsE and (B) for the S-layer protein rSgsE.

Mentions: In addition, QCM-D is also sensitive to changes in the viscoelasticity of the film adhering to the sensor crystal. These factors must be considered for the conversion of frequency shifts to mass change [42]. Besides the increase in mass (Fig. 3B), also the change in dissipation has been determined for wtSgsE and rSgsE at a concentration of 50 μg mL−1 (Fig. 4). Interestingly, for the glycoprotein wtSgsE the shift in dissipation was large compared to rSgsE and an exponential approximation to the final value of 4.5 × 10−6 was determined (Table 1; Fig. 4A). In contrast, the shift in dissipation was much smaller for the S-layer protein rSgsE as a final value of 0.79 × 10−6 was observed (Table 1; Fig. 4B).


Relevance of glycosylation of S-layer proteins for cell surface properties.

Schuster B, Sleytr UB - Acta Biomater (2015)

Recrystallization process of two different S-layer (glyco)proteins from Geobacillus stearothermophilus NRS 2004/3a (protein concentration of 50 μg mL−1) on gold-covered sensor surfaces as followed by quartz crystal microbalance with dissipation monitoring (QCM-D). The shift in frequency (left axis) and dissipation (right axis) as a function of time at the 5th overtone is shown for (A) the S-layer glycoprotein wtSgsE and (B) for the S-layer protein rSgsE.
© Copyright Policy - CC BY
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4414373&req=5

f0020: Recrystallization process of two different S-layer (glyco)proteins from Geobacillus stearothermophilus NRS 2004/3a (protein concentration of 50 μg mL−1) on gold-covered sensor surfaces as followed by quartz crystal microbalance with dissipation monitoring (QCM-D). The shift in frequency (left axis) and dissipation (right axis) as a function of time at the 5th overtone is shown for (A) the S-layer glycoprotein wtSgsE and (B) for the S-layer protein rSgsE.
Mentions: In addition, QCM-D is also sensitive to changes in the viscoelasticity of the film adhering to the sensor crystal. These factors must be considered for the conversion of frequency shifts to mass change [42]. Besides the increase in mass (Fig. 3B), also the change in dissipation has been determined for wtSgsE and rSgsE at a concentration of 50 μg mL−1 (Fig. 4). Interestingly, for the glycoprotein wtSgsE the shift in dissipation was large compared to rSgsE and an exponential approximation to the final value of 4.5 × 10−6 was determined (Table 1; Fig. 4A). In contrast, the shift in dissipation was much smaller for the S-layer protein rSgsE as a final value of 0.79 × 10−6 was observed (Table 1; Fig. 4B).

Bottom Line: Interestingly, to the wtSgsE lattice almost twice the amount of water is bound and/or coupled in comparison with the non-glycosylated rSgsE with the preferred region being the extending glycan residues.The present results are discussed in terms of the effect of the glycan residues on the recrystallization, the adjoining hydration layer, and the nanoscale roughness and fluidic behavior.The latter features may turn out to be one of the most general ones among bacterial and archaeal S-layer lattices.

View Article: PubMed Central - PubMed

Affiliation: Institute for Synthetic Bioarchitectures, Department of NanoBiotechnology, University of Natural Resources and Life Sciences, Vienna, Muthgasse 11, 1190 Vienna, Austria. Electronic address: bernhard.schuster@boku.ac.at.

Show MeSH
Related in: MedlinePlus