This article is part of the supplement: The 4th Recombinant Protein Production Meeting: a comparative view on host physiology .

Poster Presentation

Efficient, antibody-mediated allosteric activation of an immobilized, E. coli beta-galactosidase recombinant biosensor

Rosa M Ferraz^1,3, Anna Arís¹, Gregorio Álvaro² and Antonio Villaverde¹

¹  Institut de Biotecnologia i de Biomedicina and Departament de Genètica i de Microbiologia, Universitat Autònoma de Barcelona, Bellaterra, 08193 Barcelona, Spain

²  Departament d' Enginyeria Química, Universitat Autònoma de Barcelona, Bellaterra, 08193 Barcelona, Spain

³  Departament de Matemàtica Aplicada IV, Universitat Politècnica de Catalunya. Campus Nord, Jordi Girona 1-3, 08034, Barcelona, Spain

corresponding author email

from The 4th Recombinant Protein Production Meeting: a comparative view on host physiology
Barcelona, Spain. 21–23 September 2006

Microbial Cell Factories 2006, 5(Suppl 1):P43doi:10.1186/1475-2859-5-S1-P43

Published:	10 October 2006

First paragraph (this article has no abstract)

Allosteric biosensors are based on engineered reporter enzymes responsive to analyte binding through detectable changes in the specific activity [1,2]. Since antibodies are efficient allosteric effectors, such devices are especially useful for the diagnosis of infectious diseases. In previous studies, we have introduced an antigenic peptide from the HIV structural protein gp41, spanning amino acids 579 to 613 of the Env precursor [3], into a permissive site of E. coli beta-galactosidase, resulting in the chimeric protein NF795gpC. In the presence of immune sera or anti-peptide antibodies, the soluble enzyme is efficiently activated in a fast and homogeneous immunoassay [3,4]. To further develop biosensor devices in solid phases, with wider applicability in field conditions, we have here explored the allosteric properties of NF795gpC when immobilized in an agarose substrate.