Selection by phage display of llama conventional V(H) fragments with heavy chain antibody V(H)H properties: J.Immunol.Methods

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TypeArticle
Journal titleJournal of Immunological Methods
Volume263
Issue1-2
Pages97109; # of pages: 13
SubjectAmino Acid Sequence; Animals; Antibodies; Base Sequence; Camelids,New World; DNA,Complementary; Escherichia coli; ESCHERICHIA-COLI; genetics; Human; Immunoglobulin Fragments; Immunoglobulin Variable Region; Immunoglobulins,Heavy-Chain; immunology; Molecular Sequence Data; Oligonucleotide Probes; Peptide Library; Sequence Homology,Amino Acid; Solubility; Temperature
AbstractA llama single domain antibody (dAb) library designed and constructed to contain only heavy chain antibody variable domains (V(H)Hs) also contained a substantial number of typical conventional antibody heavy chain variable sequences (V(H)s). Panning the library against two carbohydrate-specific antibodies yielded anti-idiotypic dAbs and enriched solely for sequences from the V(H) subpopulation of the library. The conventional antibody origin of these V(H)s was confirmed by using oligonucleotide probes, specific for the enriched V(H)s, to identify the parental sequences in the message employed in library construction. Surprisingly, these V(H) dAbs, which are produced in high yield in Escherichia coli, are highly soluble, have excellent temperature stability profiles and do not display any aggregation tendencies. The very close similarity of these molecules to human V(H)s makes them potentially very useful as therapeutic dAbs
Publication date
LanguageEnglish
AffiliationNRC Institute for Biological Sciences; National Research Council Canada
Peer reviewedNo
NRC numberTANHA2002B
NPARC number9368683
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Record identifier13734729-7d5b-4b35-aa11-4cf09d90bc44
Record created2009-07-10
Record modified2016-05-09
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