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Binding activities of a repertoire of single immunoglobulin variable domains secreted from Escherichia coli

Binding activities of a repertoire of single immunoglobulin variable domains secreted from Escherichia coli
Binding activities of a repertoire of single immunoglobulin variable domains secreted from Escherichia coli

IN antibodies, a heavy and a light chain variable domain, VH and VL, respectively, pack together and the hypervariable loops on each domain contribute to binding antigen. We find, however, that isolated VH domains with good antigen-binding affinities can also be prepared. Using the polymerase chain reaction, diverse libraries of VH genes were cloned from the spleen genomic DNA of mice immunized with either lysozyme or keyhole-limpet haemocyanin. From these libraries, VH domains were expressed and secreted from Escherichia coli. Binding activities were detected against both antigens, and two VH domains were characterized with affinities for lysozyme in the 20 nM range. Isolated variable domains may offer an alternative to monoclonal antibodies and serve as the key to building high-affinity human antibodies. We suggest the name 'single domain antibodies (dAbs)' for these antigen binding demands.

0028-0836
544-546
Ward, E. Sally
b31c0877-8abe-485f-b800-244a9d3cd6cc
Güssow, Detlef
cdf213ad-dcce-4842-b16a-d1d31c30f58f
Griffiths, Andrew D.
ec264a92-eda1-4ef5-bb8f-0ebaf931425a
Jones, Peter T.
0cfdad44-bb71-46e4-8c36-a190ccdac68e
Winter, Greg
72106f71-2931-453a-861d-27625707b8fe
Ward, E. Sally
b31c0877-8abe-485f-b800-244a9d3cd6cc
Güssow, Detlef
cdf213ad-dcce-4842-b16a-d1d31c30f58f
Griffiths, Andrew D.
ec264a92-eda1-4ef5-bb8f-0ebaf931425a
Jones, Peter T.
0cfdad44-bb71-46e4-8c36-a190ccdac68e
Winter, Greg
72106f71-2931-453a-861d-27625707b8fe

Ward, E. Sally, Güssow, Detlef, Griffiths, Andrew D., Jones, Peter T. and Winter, Greg (1989) Binding activities of a repertoire of single immunoglobulin variable domains secreted from Escherichia coli. Nature, 341 (6242), 544-546. (doi:10.1038/341544a0).

Record type: Article

Abstract

IN antibodies, a heavy and a light chain variable domain, VH and VL, respectively, pack together and the hypervariable loops on each domain contribute to binding antigen. We find, however, that isolated VH domains with good antigen-binding affinities can also be prepared. Using the polymerase chain reaction, diverse libraries of VH genes were cloned from the spleen genomic DNA of mice immunized with either lysozyme or keyhole-limpet haemocyanin. From these libraries, VH domains were expressed and secreted from Escherichia coli. Binding activities were detected against both antigens, and two VH domains were characterized with affinities for lysozyme in the 20 nM range. Isolated variable domains may offer an alternative to monoclonal antibodies and serve as the key to building high-affinity human antibodies. We suggest the name 'single domain antibodies (dAbs)' for these antigen binding demands.

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Published date: 12 October 1989

Identifiers

Local EPrints ID: 425254
URI: http://eprints.soton.ac.uk/id/eprint/425254
ISSN: 0028-0836
PURE UUID: 616de0c2-72fa-4dea-9922-0152927f523c
ORCID for E. Sally Ward: ORCID iD orcid.org/0000-0003-3232-7238

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Date deposited: 12 Oct 2018 16:30
Last modified: 07 Oct 2020 02:22

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Contributors

Author: E. Sally Ward ORCID iD
Author: Detlef Güssow
Author: Andrew D. Griffiths
Author: Peter T. Jones
Author: Greg Winter

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