About: Comparison of the efficiency of antibody selection from semi-synthetic scFv and non-immune Fab phage display libraries against protein targets for rapid development of diagnostic immunoassays

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About: Comparison of the efficiency of antibody selection from semi-synthetic scFv and non-immune Fab phage display libraries against protein targets for rapid development of diagnostic immunoassays Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Comparison of the efficiency of antibody selection from semi-synthetic scFv and non-immune Fab phage display libraries against protein targets for rapid development of diagnostic immunoassays
Creator	Chan, Annie Hanson, Brendon Lim, Angeline Chan, Conrad
Source	Elsevier; Medline; PMC
abstract	Abstract Rapid development of diagnostic immunoassays against novel emerging or genetically modified pathogens in an emergency situation is dependent on the timely isolation of specific antibodies. Non-immune antibody phage display libraries are an efficient in vitro method for selecting monoclonal antibodies and hence ideal in these circumstances. Such libraries can be constructed from a variety of sources e.g. B cell cDNA or synthetically generated, and use a variety of antibody formats, typically scFv or Fab. However, antibody source and format can impact on the quality of antibodies generated and hence the effectiveness of this methodology for the timely production of antibodies. We have carried out a comparative screening of two antibody libraries, a semi-synthetic scFv library and a human-derived Fab library against the protective antigen toxin component of Bacillus anthracis and the epsilon toxin of Clostridium botulinum. We have shown that while the synthetic library produced a diverse collection of specific scFv-phage, these contained a high frequency of unnatural amber stops and glycosylation sites which limited their conversion to IgG, and also a high number which lost specificity when expressed as IgG. In contrast, these limitations were overcome by the use of a natural human library. Antibodies from both libraries could be used to develop sandwich ELISA assays with similar sensitivity. However, the ease and speed with which full-length IgG could be generated from the human-derived Fab library makes screening this type of library the preferable method for rapid antibody generation for diagnostic assay development.
has issue date	2011-10-28(xsd:dateTime)
bibo:doi	10.1016/j.jim.2011.08.005
bibo:pmid	21856306
has license	els-covid
sha1sum (hex)	fbef2a6b40647fe55f4c6d2e082d1624eeb63741
schema:url	https://doi.org/10.1016/j.jim.2011.08.005
resource representing a document's title	Comparison of the efficiency of antibody selection from semi-synthetic scFv and non-immune Fab phage display libraries against protein targets for rapid development of diagnostic immunoassays
has PubMed Central identifier	PMC7094349
has PubMed identifier	21856306
schema:publication	Journal of Immunological Methods
resource representing a document's body	covid:fbef2a6b40647fe55f4c6d2e082d1624eeb63741#body_text
is schema:about of	named entity 'RAPID' named entity 'limitations' named entity 'scFv' named entity 'conversion' named entity 'library' named entity 'genetically modified' named entity 'Fab' named entity 'antibody' named entity 'IgG' named entity 'expressed' named entity 'contrast' named entity 'specific' named entity 'COMPARISON' named entity 'DEVELOPMENT' named entity 'PHAGE' named entity 'EFFECTIVENESS' named entity 'SCFV' named entity 'HUMAN' named entity 'IN VITRO' named entity 'GENERATED' named entity 'MODIFIED' named entity 'LIBRARY' named entity 'LIBRARIES' named entity 'SELECTING' named entity 'OVERCOME' named entity 'DERIVED' named entity 'SOURCE' named entity 'THESE' named entity 'SENSITIVITY' named entity 'EPSILON TOXIN' named entity 'EXPRESSED' named entity 'BACILLUS ANTHRACIS' named entity 'LIMITATIONS' named entity 'RAPID' named entity 'NON-' named entity 'EFFICIENCY' named entity 'LIBRARIES' named entity 'IMMUNOASSAYS' named entity 'SCFV' named entity 'CARRIED' named entity 'USE' named entity 'COMPONENT' named entity 'HIGH' named entity 'NOVEL' named entity 'DIAGNOSTIC ASSAY' named entity 'SYNTHETIC' named entity 'COULD BE' named entity 'IMMUNE' named entity 'PHAGE DISPLAY' named entity 'SYNTHETIC' named entity 'TARGETS' named entity 'NON-' named entity 'FAB' named entity 'ANTIBODY' named entity 'EFFICIENT' named entity 'DIAGNOSTIC' named entity 'DEVELOPMENT' named entity 'FORMATS' named entity 'TYPE' named entity 'PROTECTIVE ANTIGEN ' named entity 'HAVE' named entity 'THEIR' named entity 'LOST' named entity 'METHOD' named entity 'LIMITED' named entity 'ELISA ASSAYS' named entity 'MONOCLONAL ANTIBODIES' named entity 'PROTEIN ' named entity 'UNNATURAL' named entity 'QUALITY' named entity 'B CELL' named entity 'FAB' named entity 'CONTAINED' named entity 'USED' named entity 'TOXIN' named entity 'COLLECTION' named entity 'GLYCOSYLATION' named entity 'DIAGNOSTIC'

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