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Screening of phage-displayed peptide libraries with a monoclonal antibody raised against the F protein of the bovine respiratory syncytial virus

✍ Scribed by Pascal Mertens; Jean-Philippe Matheise; Bernadette Lichtfouse; Chantal Clavareau; Jean-Jacques Letesson

Publisher: Springer Netherlands
Year: 1995
Tongue: English
Weight: 365 KB
Volume: 2
Category: Article
ISSN: 1573-3149
DOI: 10.1007/bf00119158

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✦ Synopsis

Most of the monoclonal antibodies (MAbs) raised against the fusion (F) protein of the bovine respiratory syncytial virus recognize discontinuous epitopes on the protein. In order to find mimotopes of these epitopes, phage-displayed peptide libraries were screened with MAbs. The results obtained with MAb ALl 1C2 are described here. After four or five pannings, colony immunoscreening with ALl 1C2 allowed the isolation of positive clones that are specific for this monoclonal antibody. Four different sequences were determined on isolated phages, three of which are cysteine-constrained peptides in fusion with PVIII and one is a hexapeptide in fusion with PIII. In the case of the peptides containing two cysteines, the binding to ALllC2 was shown to be dependent on the presence of a disulfide bridge. The recombinant phages were also shown to inhibit the binding of ALl 1C2 to its natural antigen in a competitive ELISA assay.

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