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Article type: Research Article
Authors: Steinbergs, Jurisa | Kilchewska, Katarzinaa | Lazdina, Unaa | Dishlers, Andrisa | Ose, Veltaa | Sällberg, Mattib | Tsimanis, Alexandera; *
Affiliations: [a] Biomedical Research and Study Centre, University of Latvia, LV-1067, Kirhensteina str. 1, Riga, Latvia | [b] Department of Clinical Virology, F69, Karolinska Institutet, Huddinge University Hospital, S-14186, Stockholm, Sweden
Correspondence: [*] Correspondence and reprint requests to Alexander Tsimanis, Biomedical Research and Study Centre, University of Latvia, LV-1067, Ratsupites str. 1, Riga, Latvia.
Abstract: The construction of a mouse hybridoma FR52 secreting neutralizing monoclonal antibody specific for RNA bacteriophages fr, MS2 and GA is reported. The genes encoding the variable domains of the monoclonal antibody FR52 heavy and light chains were cloned and sequenced and the corresponding complementarity determining region (CDR) peptides were chemically synthesized. The CDR-peptides were tested for their ability to neutralize the activity of RNA phage fr and related RNA phages MS2 and GA. The CDR-derived peptides H2, L2 and L3 interacted with the fr phage particles and neutralized fr phage activity. Two of these peptides–H2 and L3 also had the ability to neutralize partly the activity of related bacteriophage MS2; but L1 and especially L3 neutralize the activity of the RNA phage GA. These results provide an excellent system for further antibody-antigen interaction studies and raise the possibility that simple CDR-peptides may serve as a new class of antiviral molecules.
Keywords: RNA phage, monoclonal antibody, synthetic CDR-peptide, phage neutralization
DOI: 10.3233/HAB-1996-7303
Journal: Human Antibodies, vol. 7, no. 3, pp. 106-112, 1996
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