6533b82bfe1ef96bd128d7f4
RESEARCH PRODUCT
Short synthetic CDR-peptides forming the antibody combining site of the monoclonal antibody against RNA bacteriophage fr neutralize the phage activity.
Alexander TsimanisKatarzina KilchewskaUna LazdinaMatti SällbergJuris SteinbergsVelta OseAndris Dishlerssubject
medicine.drug_classvirusesImmunologyMolecular Sequence DataImmunoglobulin Variable Regionchemical and pharmacologic phenomenaEnzyme-Linked Immunosorbent AssayComplementarity determining regionRNA PhagesMonoclonal antibodyBacteriophageMiceAntigenNeutralization TestsBacteriophage MS2medicineImmunology and AllergyAnimalsAmino Acid SequenceCloning MolecularMicroscopy ImmunoelectronMice Inbred BALB CbiologyBase SequenceRNAAntibodies MonoclonalGeneral MedicineRNA Phagesbiology.organism_classificationMolecular biologyPeptide Fragmentsbiology.proteinAntibodydescription
The construction of a mouse hybridoma FRS2 secreting neutralizing monoclonal antibody specific for RNA bacteriophages fr, MS2 and GA is reported. The genes encoding the variable domains of the monoclonal antibody FRS2 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; butLJande-speciilll'y 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 anti viral molecules. [Hum Antibod Hybridomas 1996; 7: 106-112]
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1996-09-01 | Human antibodies and hybridomas |