High stability of trehalose/maltose binding protein fromThermococcus litoralismakes it a good candidate as a sensitive element in biosensor systems for sugar control

Fluorescence and circular dichroism in far-UV region were used to study the stability of trehalose/maltose binding protein (TMBP) from hyper thermophilic archaeonThermococcus litoralisand its complex with glucose (TMBP/Glc). The evaluation of difference between free energy of native and unfolded state for TMBP and TMBP/Glc showed that both of them are several times higher than that of proteins from mesophilic organisms. Due to the high stability and innate ability to bind glucose this protein is a good candidate as a sensitive element in biosensor systems for sugar control.

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Effect of Signal Peptide on the Stability and Folding Kinetics of Maltose Binding Protein†

Biochemistry ◽

10.1021/bi0360509 ◽

2004 ◽

Vol 43 (12) ◽

pp. 3608-3619 ◽

Cited By ~ 43

Author(s):

K. Beena ◽

Jayant B. Udgaonkar ◽

R. Varadarajan

Keyword(s):

Signal Peptide ◽

Binding Protein ◽

Maltose Binding Protein ◽

Folding Kinetics ◽

The Stability ◽

Kinetics Of

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Potential Role for Toll-Like Receptor 4 in Mediating Escherichia coli Maltose-Binding Protein Activation of Dendritic Cells

Infection and Immunity ◽

10.1128/iai.00486-06 ◽

2007 ◽

Vol 75 (3) ◽

pp. 1359-1363 ◽

Cited By ~ 28

Author(s):

Stefan Fernandez ◽

Dupeh R. Palmer ◽

Monika Simmons ◽

Peifang Sun ◽

John Bisbing ◽

...

Keyword(s):

Escherichia Coli ◽

Dendritic Cells ◽

Pathogenic Bacteria ◽

Binding Protein ◽

Maltose Binding Protein ◽

Toll Like Receptor ◽

Toll Like Receptor 4 ◽

Necrosis Factor Alpha ◽

Protein Activation ◽

The Stability

ABSTRACT The Escherichia coli maltose-binding protein (MBP) is used to increase the stability and solubility of proteins in bacterial protein expression systems and is increasingly being used to facilitate the production and delivery of subunit vaccines against various pathogenic bacteria and viruses. The MBP tag is presumed inert, with minimum effects on the bioactivity of the tagged protein or its biodistribution. However, few studies have characterized the immunological attributes of MBP. Here, we analyze the phenotypic and functional outcomes of MBP-treated dendritic cells (DCs) and show that MBP induces DC activation and production of proinflammatory cytokines (interleukin-1β [IL-1β], IL-6, IL-8, tumor necrosis factor alpha, and IL-12p70) within 24 h and strongly increases Iκβ phosphorylation in treated cells. Interestingly, phosphorylation of Iκβ was largely abrogated by the addition of anti-human Toll-like receptor 4 (TLR4) antibodies, indicating that MBP activates signaling for DC maturation via TLR4. Consistent with this hypothesis, MBP activated the TLR4-expressing cell line 293-hTLR4A but not control cultures to secrete IL-8. The observed data were independent of lipopolysaccharide contamination and support a role for TLR4 in mediating the effects of MBP. These results provide insight into a mechanism by which MBP might enhance immune responses to vaccine fusion proteins.

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