Recombinant single-chain Fv antibodies that recognize the p25 protein of the Maedi-Visna virus
Language English Country United States Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
12879760
DOI
10.1007/bf02931380
Knihovny.cz E-resources
- MeSH
- Immunoglobulin Fragments genetics immunology isolation & purification MeSH
- Kinetics MeSH
- Immunoglobulin Light Chains genetics immunology MeSH
- Molecular Sequence Data MeSH
- Peptide Library MeSH
- Recombinant Proteins genetics immunology isolation & purification MeSH
- Amino Acid Sequence MeSH
- Base Sequence MeSH
- Sequence Analysis, DNA MeSH
- Immunoglobulin Heavy Chains genetics immunology MeSH
- Immunoglobulin Variable Region genetics immunology isolation & purification MeSH
- Capsid Proteins genetics immunology MeSH
- Visna-maedi virus genetics immunology MeSH
- Animals MeSH
- Check Tag
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Immunoglobulin Fragments MeSH
- Immunoglobulin Light Chains MeSH
- Peptide Library MeSH
- Recombinant Proteins MeSH
- Immunoglobulin Heavy Chains MeSH
- Immunoglobulin Variable Region MeSH
- Capsid Proteins MeSH
Single chain Fv (scFv) antibodies (generated by phage display technology, molecules representing new and efficient tools in the research and diagnostics of infectious diseases) against the capsid protein (p25) of Maedi-Visna virus were selected. Several clones of p25 specific scFv antibodies were identified; one of them was expressed as a soluble scFv molecule, purified by immobilized metal-affinity chromatography and further characterized by sequencing and determination of the kinetic equilibrium association constant. Sequence analysis showed that the rearranged VL and VH domains of the analyzed scFv clone used sequences from the VL3 family (germline DPL16/VL3.1) and VH1 family (germline VH20), respectively. The kinetic equilibrium association constant was determined as KA = 1.12 +/- 0.52 L/mumol.
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