Allosteric molecular sensing of anti-HIV antibodies by an immobilized engineered β-galactosidase

R. M. Ferraz; A. Aris; G. González; J. López-Santín; A. Villaverde; G. Álvaro

doi:https://doi.org/10.1016/j.enzmictec.2007.04.001

Allosteric molecular sensing of anti-HIV antibodies by an immobilized engineered β-galactosidase

R. M. Ferraz, A. Aris, G. González, J. López-Santín, A. Villaverde, G. Álvaro

Research output: Contribution to journal › Article › Research › peer-review

3 Citations (Scopus)

Abstract

The main objective is to demonstrate the feasibility of qualitative and semi-quantitative determination of anti-HIV antibodies, based on the allosteric response of an immobilized engineered Escherichia coli β-galactosidase. The suitability of this enzyme and the conditions for homogeneous assay had been previously demonstrated. In the present work, the operational conditions for engineered E. coli β-galactosidase immobilization on activated agarose supports have been determined. A solid biocatalyst has been prepared and characterized in order to determine the activation degree of the immobilized enzyme in the presence of anti-HIV antibodies. The solid-phase biocatalyst has been shown to be able to modulate its activity and produce an unequivocal signal in presence of anti-HIV containing sera from different patients. Finally, the conceptual design of a possible assay based on the above methodology is proposed. © 2007 Elsevier Inc. All rights reserved.

Original language	English
Pages (from-to)	492-497
Journal	Enzyme and Microbial Technology
Volume	41
DOIs	https://doi.org/10.1016/j.enzmictec.2007.04.001
Publication status	Published - 3 Sep 2007

Keywords

Allosteric enzymes
Anti-HIV antibodies sensing
Immobilized engineered β-galactosidase

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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https://doi.org/10.1016/j.enzmictec.2007.04.001

Cite this

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title = "Allosteric molecular sensing of anti-HIV antibodies by an immobilized engineered β-galactosidase",

abstract = "The main objective is to demonstrate the feasibility of qualitative and semi-quantitative determination of anti-HIV antibodies, based on the allosteric response of an immobilized engineered Escherichia coli β-galactosidase. The suitability of this enzyme and the conditions for homogeneous assay had been previously demonstrated. In the present work, the operational conditions for engineered E. coli β-galactosidase immobilization on activated agarose supports have been determined. A solid biocatalyst has been prepared and characterized in order to determine the activation degree of the immobilized enzyme in the presence of anti-HIV antibodies. The solid-phase biocatalyst has been shown to be able to modulate its activity and produce an unequivocal signal in presence of anti-HIV containing sera from different patients. Finally, the conceptual design of a possible assay based on the above methodology is proposed. {\textcopyright} 2007 Elsevier Inc. All rights reserved.",

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author = "Ferraz, {R. M.} and A. Aris and G. Gonz{\'a}lez and J. L{\'o}pez-Sant{\'i}n and A. Villaverde and G. {\'A}lvaro",

year = "2007",

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doi = "https://doi.org/10.1016/j.enzmictec.2007.04.001",

language = "English",

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T1 - Allosteric molecular sensing of anti-HIV antibodies by an immobilized engineered β-galactosidase

AU - Ferraz, R. M.

AU - Aris, A.

AU - González, G.

AU - López-Santín, J.

AU - Villaverde, A.

AU - Álvaro, G.

PY - 2007/9/3

Y1 - 2007/9/3

N2 - The main objective is to demonstrate the feasibility of qualitative and semi-quantitative determination of anti-HIV antibodies, based on the allosteric response of an immobilized engineered Escherichia coli β-galactosidase. The suitability of this enzyme and the conditions for homogeneous assay had been previously demonstrated. In the present work, the operational conditions for engineered E. coli β-galactosidase immobilization on activated agarose supports have been determined. A solid biocatalyst has been prepared and characterized in order to determine the activation degree of the immobilized enzyme in the presence of anti-HIV antibodies. The solid-phase biocatalyst has been shown to be able to modulate its activity and produce an unequivocal signal in presence of anti-HIV containing sera from different patients. Finally, the conceptual design of a possible assay based on the above methodology is proposed. © 2007 Elsevier Inc. All rights reserved.

AB - The main objective is to demonstrate the feasibility of qualitative and semi-quantitative determination of anti-HIV antibodies, based on the allosteric response of an immobilized engineered Escherichia coli β-galactosidase. The suitability of this enzyme and the conditions for homogeneous assay had been previously demonstrated. In the present work, the operational conditions for engineered E. coli β-galactosidase immobilization on activated agarose supports have been determined. A solid biocatalyst has been prepared and characterized in order to determine the activation degree of the immobilized enzyme in the presence of anti-HIV antibodies. The solid-phase biocatalyst has been shown to be able to modulate its activity and produce an unequivocal signal in presence of anti-HIV containing sera from different patients. Finally, the conceptual design of a possible assay based on the above methodology is proposed. © 2007 Elsevier Inc. All rights reserved.

KW - Allosteric enzymes

KW - Anti-HIV antibodies sensing

KW - Immobilized engineered β-galactosidase

U2 - https://doi.org/10.1016/j.enzmictec.2007.04.001

DO - https://doi.org/10.1016/j.enzmictec.2007.04.001

M3 - Article

VL - 41

SP - 492

EP - 497

ER -

Allosteric molecular sensing of anti-HIV antibodies by an immobilized engineered β-galactosidase

Abstract

Keywords

UN SDGs

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