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Visualization of the membrane engineering concept: evidence for the specific orientation of electroinserted antibodies and selective binding of target analytes.
J Mol Recognit
December 2013
Department of Biotechnology, Agricultural University of Athens, Iera Odos 75, 11855, Athens, Greece.
Membrane engineering is a generic methodology for increasing the selectivity of a cell biosensor against a target molecule, by electroinserting target-specific receptor-like molecules on the cell surface. Previous studies have elucidated the biochemical aspects of the interaction between various analytes (including viruses) and their homologous membrane-engineered cells. In the present study, purified anti-biotin antibodies from a rabbit antiserum along with in-house prepared biotinylated bovine serum albumin (BSA) were used as a model antibody-antigen pair of molecules for facilitating membrane engineering experiments.
View Article and Find Full Text PDFEngineering of the membrane of fibroblast cells with virus-specific antibodies: A novel biosensor tool for virus detection.
Biosens Bioelectron
December 2008
Laboratory of Plant Physiology, Faculty of Biotechnology, Agricultural University of Athens, Iera Odos 75, 11855 Athens, Greece; EMBIO Diagnostics, Nicosia, Cyprus.
A novel concept for the assay of viral antigens is described. The methodological approach is based on a membrane-engineering process involving the electroinsertion of virus-specific antibodies in the membranes of fibroblast cells. As a representative example, Vero fibroblasts were engineered with antibodies against Cucumber mosaic virus (CMV) and used for the construction of an ultra-sensitive miniature cell biosensor system.
View Article and Find Full Text PDFElectroinsertion and activation of the C-terminal domain of colicin A, a voltage gated bacterial toxin, into mammalian cell membranes.
Mol Membr Biol
May 2005
Institut de Pharmacologie et de Biologie Structurale du CNRS (UMR 5089), 205 route de Narbonne, F-31077 Toulouse cedex 4, France.
The C-terminal fragment of colicin, a protein that is highly soluble in aqueous solution, is spontaneously and irreversibly inserted into the membranes of mammalian cells, which are locally permeabilized by a transmembrane voltage increase. Insertion is detected by immunodetection. This is obtained by mixing the protein with electropermeabilized cells.
View Article and Find Full Text PDFIn vivo induction of human immunodeficiency virus type 1 entry into nucleus-free cells by CD4 gene transfer to hematopoietic stem cells: a hypothetical possible strategy for therapeutic intervention.
Med Hypotheses
July 2002
Nagahama Shinryojyo, Shimokoshiki-mura, Satsuma-gun, Kagoshima, Japan.
As a useful alternative to employing soluble CD4 to inhibit binding of human immunodeficiency virus type 1 (HIV-1) to target cells, the introduction of CD4-bearing erythrocyte has been proposed by two study groups (see Refs. (5,6)). Prominently, Nicolau and colleagues demonstrated that the electroinserted CD4 molecules in the membranes of erythrocytes are capable of mediating HIV-1 entry.
View Article and Find Full Text PDFN-linked oligosaccharides can protect target cells from the lysis mediated by NK cells but not by cytotoxic T lymphocytes: role of NKG2-A.
Tissue Antigens
August 1999
INSERM U 466, Institut Louis Bugnard, CHU Ranguell, Toulouse, France.
We have previously shown that glycophorin A (GPA), inserted by electropulsation into the membrane of K562 cells, protected them from natural killer (NK) cell-mediated cytotoxicity and the unique N-linked oligosaccharide of GPA was essential for resistance to occur. The present study demonstrates that the protection level conferred by GPA is similar to the resistance induced by HLA-Cw3 expressed by transfected K562 cells. A monoclonal antibody against NKG2-A, an NK inhibitory receptor interacting with HLA class I antigens and belonging to the C-type lectin receptor, was able to restore the ability of NK cells to lyse K562 cells expressing HLA-Cw3 at the cell membrane but not electroinserted-GPA, suggesting that the N-linked oligosaccharide of GPA cannot be a ligand for NKG2-A.
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