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Escherichia coli with autodisplayed Z-domain of protein A for signal amplification of SPR biosensor.
Biosens Bioelectron. 2009 Jan 01; 24(5):1324-9.BB

Abstract

Generally, an immunoaffinity SPR biosensor detects a target analyte in a sample through highly selective adsorption by using the antigen-antibody interaction. For improving the sensitivity, various kinds of particles have been added to the already bound analytes on the SPR biosensor (sandwich assay). In this work, signal amplification was demonstrated by the expression of the IgG-binding Z-domain of protein A on the outer membrane of Escherichia coli via "Autodisplay". The amount of Z-domain of protein A expressed on the outer membrane was calculated to be 280,000 molecules per cell. In addition, the IgG-binding ability of the expressed protein was characterized using FACS analysis. The signal amplification of the SPR biosensor was performed in the sandwich assay format using a model of horseradish peroxidase (HRP); the limit of detection was determined to be significantly improved from 1 microg/ml to 1 ng/ml. Finally, myoglobin analysis was demonstrated for the medical diagnosis of cardiac diseases. The detection limit was estimated to be improved from 10 ng/ml to <1 ng/ml. These results show that Z-domain-displaying E. coli can be successfully used for the signal amplification of immunoaffinity biosensors, thereby improving the sensitivity and the limit of detection.

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Authors+Show Affiliations

Jose J
Institute of Pharmaceutical and Medicinal Chemistry, Heinrich Heine University, Duesseldorf, Germany.
Chung JW
No affiliation info available
Jeon BJ
No affiliation info available
Maas RM
No affiliation info available
Nam CH
No affiliation info available
Pyun JC
No affiliation info available

MeSH

Biological AssayBiosensing TechniquesEquipment DesignEquipment Failure AnalysisEscherichia coliImmunoassayImmunoglobulin GProtein EngineeringProtein Structure, TertiaryReproducibility of ResultsSensitivity and SpecificityStaphylococcal Protein ASurface Plasmon Resonance

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

19036573

Citation

Jose, Joachim, et al. "Escherichia Coli With Autodisplayed Z-domain of Protein a for Signal Amplification of SPR Biosensor." Biosensors & Bioelectronics, vol. 24, no. 5, 2009, pp. 1324-9.
Jose J, Chung JW, Jeon BJ, et al. Escherichia coli with autodisplayed Z-domain of protein A for signal amplification of SPR biosensor. Biosens Bioelectron. 2009;24(5):1324-9.
Jose, J., Chung, J. W., Jeon, B. J., Maas, R. M., Nam, C. H., & Pyun, J. C. (2009). Escherichia coli with autodisplayed Z-domain of protein A for signal amplification of SPR biosensor. Biosensors & Bioelectronics, 24(5), 1324-9. https://doi.org/10.1016/j.bios.2008.07.067
Jose J, et al. Escherichia Coli With Autodisplayed Z-domain of Protein a for Signal Amplification of SPR Biosensor. Biosens Bioelectron. 2009 Jan 1;24(5):1324-9. PubMed PMID: 19036573.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Escherichia coli with autodisplayed Z-domain of protein A for signal amplification of SPR biosensor. AU - Jose,Joachim, AU - Chung,Ji-Won, AU - Jeon,Byoung-Jin, AU - Maas,Ruth Maria, AU - Nam,Chang-Hoon, AU - Pyun,Jae-Chul, Y1 - 2008/08/08/ PY - 2008/04/14/received PY - 2008/07/14/revised PY - 2008/07/24/accepted PY - 2008/11/28/pubmed PY - 2009/3/10/medline PY - 2008/11/28/entrez SP - 1324 EP - 9 JF - Biosensors & bioelectronics JO - Biosens Bioelectron VL - 24 IS - 5 N2 - Generally, an immunoaffinity SPR biosensor detects a target analyte in a sample through highly selective adsorption by using the antigen-antibody interaction. For improving the sensitivity, various kinds of particles have been added to the already bound analytes on the SPR biosensor (sandwich assay). In this work, signal amplification was demonstrated by the expression of the IgG-binding Z-domain of protein A on the outer membrane of Escherichia coli via "Autodisplay". The amount of Z-domain of protein A expressed on the outer membrane was calculated to be 280,000 molecules per cell. In addition, the IgG-binding ability of the expressed protein was characterized using FACS analysis. The signal amplification of the SPR biosensor was performed in the sandwich assay format using a model of horseradish peroxidase (HRP); the limit of detection was determined to be significantly improved from 1 microg/ml to 1 ng/ml. Finally, myoglobin analysis was demonstrated for the medical diagnosis of cardiac diseases. The detection limit was estimated to be improved from 10 ng/ml to <1 ng/ml. These results show that Z-domain-displaying E. coli can be successfully used for the signal amplification of immunoaffinity biosensors, thereby improving the sensitivity and the limit of detection. SN - 1873-4235 UR - https://www.unboundmedicine.com/medline/citation/19036573/Escherichia_coli_with_autodisplayed_Z_domain_of_protein_A_for_signal_amplification_of_SPR_biosensor_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0956-5663(08)00412-0 DB - PRIME DP - Unbound Medicine ER -