Development of an Autofluorescent Whole-Cell Biocatalyst by Displaying Dual Functional Moieties on
            <i>Escherichia coli</i>
            Cell Surfaces and Construction of a Coculture with Organophosphate-Mineralizing Activity

Yang, Chao; Zhu, Yaran; Yang, Jijian; Liu, Zheng; Qiao, Chuanling; Mulchandani, Ashok; Chen, Wilfred

doi:10.1128/aem.01936-08

Cited by 24 publications

(10 citation statements)

References 47 publications

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“…The efficiency of surface display systems and the correct and efficient protein folding and its stability is highly related to the specifications of the carrier protein, passenger protein, and fusion method (Yang. et al 2008a , b ; Barrett et al 2019 ). LPP-ompA is an efficient surface display system that has been developed and applied for various applications (Fasehee et al 2018 ; Rigi et al 2014 ; Tafakori et al 2012 ).…”

Section: Discussionmentioning

confidence: 98%

“…Display of heterologous proteins on the bacterial surface has been demonstrated as a multi-strategy approach to develop an efficient vaccine for S. aureus development (Kim et al 2010 ; Kalyanasundram et al 2015 ), screening of antibody libraries (Cavallari 2017 ), development of whole-cell bioadsorbents (Tafakori et al 2012 ), and biosensors (Furst et al 2017 ). Chimeric protein system of the Lpp′-OmpA is used as an anchor and loads heterologous proteins onto the Gram-negative bacterial surface (Yang et al 2008a , b ; Georgiou et al 1996 ). Lpp′-OmpA consists of the first nine aminoacids of the E. coli lipoprotein (Lpp) which is fused to the residues 46–159 of the OmpA porin protein family to anchor bacterial cell wall envelope (Francisco et al 1992 ; Tafakori et al 2014 ).…”

Section: Introductionmentioning

confidence: 99%

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Molecular dynamics simulation and experimental study of the surface-display of SPA protein via Lpp-OmpA system for screening of IgG

et al. 2020

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Staphylococcal protein A (SpA) is a major virulence factor of Staphylococcus aureus. S. aureus is able to escape detection by the immune system by the surface display of protein A. The SpA protein is broadly used to purify immunoglobulin G (IgG) antibodies. This study investigates the fusion ability of Lpp′-OmpA (46-159) to anchor and display five replicate domains of protein A with 295 residues length (SpA295) of S. aureus on the surface of Escherichia coli to develop a novel bioadsorbent. First, the binding between Lpp'-OmpA-SPA295 and IgGFc and the three-dimensional structure was investigated using molecular dynamics simulation. Then high IgG recovery from human serum by the surface-displayed system of Lpp′-OmpA-SPA295 performed experimentally. In silico analysis was demonstrated the binding potential of SPA295 to IgG after expression on LPP-OmpA surface. Surface-engineered E. coli displaying SpA protein and IgG-binding assay with SDS-PAGE analysis exhibited high potential of the expressed complex on the E. coli surface for IgG capture from human serum which is applicable to conventional immune precipitation.

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Section: Discussionmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

Molecular dynamics simulation and experimental study of the surface-display of SPA protein via Lpp-OmpA system for screening of IgG

et al. 2020

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“…The whole-cell GFP fluorescence was determined using a fluorescence spectrophotometer (F-4500; Hitachi, Japan) as described previously …”

Section: Methodsmentioning

confidence: 99%

Development of a Whole-Cell Biocatalyst/Biosensor by Display of Multiple Heterologous Proteins on the Escherichia coli Cell Surface for the Detoxification and Detection of Organophosphates

Liu

Yang

et al. 2013

J. Agric. Food Chem.

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This paper reports the codisplay of organophosphorus hydrolase (OPH) and methyl parathion hydrolase (MPH)-green fluorescent protein (GFP) fusion on the cell surface of Escherichia coli using the truncated ice nucleation protein (INPNC) and Lpp-OmpA as the anchoring motifs. The surface localization of both OPH and MPH-GFP was demonstrated by cell fractionation, Western blot analysis, protease accessibility experiment, and immunofluorescence microscopy. Anchorage of the foreign proteins on the outer membrane neither inhibits cell growth nor affects cell viability. The recombinant strain can be used as a whole-cell biocatalyst and showed a broader substrate range than strains expressing either OPH or MPH. A mixture of six organophosphorus pesticides (OPs) (0.2 mM each) could be degraded completely within 5 h. The broader substrate specificity in combination with the rapid degradation rate makes the recombinant strain a promising candidate for detoxification of OPs. The fluorescence of surface-displayed GFP is very sensitive to environmental pH change. Because hydrolysis of OPs by OPH or MPH generates protons, the recombinant E. coli could be used as a whole-cell biosensor for the rapid detection of OPs by evaluating fluorescence changes as a function of OP concentrations.

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“…The microbial surface display system is usually composed of a passenger protein (target protein), an anchor protein (carrier protein) and host microbes (Figure ). To date, varying anchor proteins such as ice nucleation protein (INP), Lpp-OmpA, EstA, and OmpC, and OmpA have been used. Microbial surface display is classified into phage display, yeast display, and bacterial display, which enables foreign peptides or proteins to directly interact with substrate without passing through the outer membrane by means of genetic engineering.…”

Section: Strategies For Improving Stability In Efcsmentioning

confidence: 99%

Tackling the Challenges of Enzymatic (Bio)Fuel Cells

et al. 2019

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The ever-increasing demands for clean and sustainable energy sources combined with rapid advances in bio-integrated portable or implantable electronic devices have stimulated intensive research activities in enzymatic (bio)fuel cells (EFCs). The use of renewable biocatalysts, the utilization of abundant green, safe, and high energy density fuels, together with the capability of working at modest and biocompatible conditions, make EFCs promising as next generation alternative power sources. However, the main challenges (low energy density, relatively low power density, poor operational stability and limited voltage output) hinder future applications of EFCs. This review aims at exploring the underlying mechanism of EFCs and providing possible practical strategies, methodologies and insights to tackle of these issues. Firstly, this review summarizes approaches in achieving high energy densities in EFCs, particularly, employing enzyme cascades for the deep/complete oxidation of fuels. Secondly, strategies for increasing power densities in EFCs, including increasing enzyme activities, facilitating electron transfers, employing nanomaterials, and designing more efficient enzyme-electrode interfaces, are described. The potential of EFCs/(super)capacitor combination is discussed. Thirdly, the review evaluates a range of strategies for improving the stability of EFCs, including the use of different enzyme immobilization approaches, tuning enzyme properties, designing protective matrixes, and using microbial surface displaying enzymes. Fourthly, approaches for the improvement of the cell voltage of EFCs are highlighted. Finally, future developments and a prospective on EFCs are envisioned.

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Development of an Autofluorescent Whole-Cell Biocatalyst by Displaying Dual Functional Moieties on Escherichia coli Cell Surfaces and Construction of a Coculture with Organophosphate-Mineralizing Activity

Cited by 24 publications

References 47 publications

Molecular dynamics simulation and experimental study of the surface-display of SPA protein via Lpp-OmpA system for screening of IgG

Molecular dynamics simulation and experimental study of the surface-display of SPA protein via Lpp-OmpA system for screening of IgG

Development of a Whole-Cell Biocatalyst/Biosensor by Display of Multiple Heterologous Proteins on the Escherichia coli Cell Surface for the Detoxification and Detection of Organophosphates

Tackling the Challenges of Enzymatic (Bio)Fuel Cells

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