A multivalent recombinant antibody fragment specific for carcinoembryonic antigen

In the present paper we report the development of a bivalent scFv (single‐chain Fv) antibody fragment, starting from a mouse mAb (monoclonal antibody) specific for CEA (carcinoembryonic antigen) that has received approval for in vivo radioimmunodiagnosis in humans. The diabody is well expressed in E...

Full description

Saved in:
Bibliographic Details
Published in:Biotechnology and applied biochemistry 2006-01, Vol.43 (1), p.39-48
Main Authors: Perez, Lincidio, Ayala, Marta, Pimentel, Gilmara, Bell, Hanssel, Canaán-Haden, Leonardo, Bequet, Mónica, González, Luis Javier, Miranda, Marlen, Ravelo, Rolando, Roque, Lourdes, Acevedo, Boris, Oliva, Juan P., Gavilondo, Jorge V.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Antibodies, Monoclonal - chemistry
Antibodies, Monoclonal - immunology
Antibodies, Monoclonal - pharmacokinetics
antibody
biodistribution
Biological and medical sciences
Biotechnology
carcinoembryonic antigen (CEA)
Carcinoembryonic Antigen - immunology
Cell Line, Tumor
Cloning, Molecular
diabody
Escherichia coli
Escherichia coli - genetics
Female
Fundamental and applied biological sciences. Psychology
Humans
Immunoglobulin Fragments - chemistry
Immunoglobulin Fragments - immunology
Immunoglobulin Fragments - pharmacology
Iodine Radioisotopes
Mice
Mice, Nude
Molecular Sequence Data
Neoplasm Transplantation
Neoplasms - diagnostic imaging
Neoplasms - immunology
Neoplasms - metabolism
Radioimmunodetection
Recombinant Proteins - chemistry
Recombinant Proteins - immunology
Recombinant Proteins - pharmacokinetics
single-chain Fv (scFv)
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:In the present paper we report the development of a bivalent scFv (single‐chain Fv) antibody fragment, starting from a mouse mAb (monoclonal antibody) specific for CEA (carcinoembryonic antigen) that has received approval for in vivo radioimmunodiagnosis in humans. The diabody is well expressed in Escherichia coli, is easily purified by a combination of immobilized metal ion affinity chromatography and gel filtration and exhibits high affinity and specificity for CEA, comparable with those of the original mAb. Biodistribution experiments in athymic nude mice transplanted with human CEA+ cancer cells showed that the 125I‐labelled diabody preferentially localizes in the tumour tissue and that retention is still high 48 h after injection. The diabody can be advantageous for some in vivo tumour targeting applications, due to the faster clearance derived from its smaller molecular mass.
ISSN:0885-4513
1470-8744
DOI:10.1042/BA20050073