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Epitope Mapping of Neutralizing Monoclonal Antibodies to Human Interferon-gamma Using Human-Bovine Interferon-gamma Chimeras
Stockholm University, Faculty of Science, The Wenner-Gren Institute, Immunology. Mabtech, Sweden.
Number of Authors: 4
2016 (English)In: Journal of Interferon and Cytokine Research, ISSN 1079-9907, E-ISSN 1557-7465, Vol. 36, no 9, 542-551 p.Article in journal (Refereed) Published
Abstract [en]

Our aim was to identify conformational epitopes, recognized by monoclonal antibodies (mAbs) made against human (h) interferon (IFN)-. Based on the mAbs' (n=12) ability to simultaneously bind hIFN- in ELISA, 2 epitope clusters with 5mAbs in each were defined; 2mAbs recognized unique epitopes. Utilizing the mAbs' lack of reactivity with bovine (b) IFN-, epitopes were identified using 7h/bIFN- chimeras where the helical regions (A-F) or the C terminus were substituted with bIFN- residues. Chimeras had a N-terminal peptide tag enabling the analysis of mAb recognition of chimeras in ELISA. The 2mAb clusters mapped to region A and E, respectively; the epitopes of several mAbs also involved additional regions. MAbs in cluster A neutralized, to various degrees, IFN--mediated activation of human cells, in line with the involvement of region A in the IFN- receptor interaction. MAbs mapping to region E displayed a stronger neutralizing capacity although this region has not been directly implicated in the receptor interaction. The results corroborate earlier studies and provide a detailed picture of the link between the epitope specificity and neutralizing capacity of mAbs. They further demonstrate the general use of peptide-tagged chimeric proteins as a powerful and straightforward method for efficient mapping of conformational epitopes.

Place, publisher, year, edition, pages
2016. Vol. 36, no 9, 542-551 p.
National Category
Biochemistry and Molecular Biology Medicinal Chemistry
URN: urn:nbn:se:su:diva-135044DOI: 10.1089/jir.2016.0017ISI: 000383507400003PubMedID: 27336613OAI: diva2:1044284
Available from: 2016-11-02 Created: 2016-10-31 Last updated: 2016-11-02Bibliographically approved

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