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Epitope mapping of monoclonal and polyclonal antibodies using bacterial cell surface display
KTH, School of Biotechnology (BIO), Proteomics and Nanobiotechnology.ORCID iD: 0000-0003-1096-9061
KTH, School of Biotechnology (BIO), Proteomics and Nanobiotechnology.ORCID iD: 0000-0002-1389-5371
KTH, School of Biotechnology (BIO), Proteomics and Nanobiotechnology.ORCID iD: 0000-0002-9977-5724
2014 (English)In: Monoclonal antibodies, Humana Press, 2014, 485-500 p.Chapter in book (Refereed)
Abstract [en]

The unique property of specific high-affinity binding to more or less any target of interest has made antibodies tremendously useful in numerous applications. Hence knowledge of the precise binding site (epitope) of antibodies on the target protein is one of the most important features for understanding its performance and determining its reliability in immunoassays. Here, we describe a high-resolution method for mapping epitopes of antibodies based on bacterial surface expression of antigen fragments followed by antibody-based flow cytometric sorting. Epitopes are determined by DNA sequencing of the sorted antibody-binding cells followed by sequence alignment back to the antigen sequence. The method described here has been useful for the mapping of both monoclonal and polyclonal antibodies with varying sizes of epitopes.

Place, publisher, year, edition, pages
Humana Press, 2014. 485-500 p.
Series
Methods in Molecular Biology, ISSN 1064-3745 ; 1131
Keyword [en]
Antibody, Cell surface display, Epitope mapping, FACS, Gram-positive, S. carnosus
National Category
Cell and Molecular Biology
Identifiers
URN: urn:nbn:se:kth:diva-161512PubMedID: 24515484Scopus ID: 2-s2.0-84896140138OAI: oai:DiVA.org:kth-161512DiVA: diva2:794868
Note

QC 20150313

Available from: 2015-03-13 Created: 2015-03-12 Last updated: 2017-05-19Bibliographically approved

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