Preparation and Characterization of Agonistic Monoclonal Antibodies Against Toll-Like Receptor 4-MD-2 Complex
| Autor: | Hiroki Tsukamoto, Masao Kimoto, Uleng Bahrun, Kenji Fukudome, Jun Kohara, Naoko Tsuneyoshi |
|---|---|
| Rok vydání: | 2007 |
| Předmět: |
Lipopolysaccharide
medicine.drug_class Immunology Lymphocyte Antigen 96 Mice SCID Biology Monoclonal antibody Binding Competitive Epitope Cell Line Mice chemistry.chemical_compound Immune system medicine Animals Humans Immunology and Allergy Receptor Mice Knockout Mice Inbred C3H Toll-like receptor Hybridomas Antibodies Monoclonal Molecular biology Mice Inbred C57BL Toll-Like Receptor 4 chemistry biology.protein TLR4 Binding Sites Antibody Antibody Protein Binding |
| Zdroj: | Hybridoma. 26:393-400 |
| ISSN: | 1557-8348 1554-0014 |
| DOI: | 10.1089/hyb.2007.0523 |
| Popis: | Ligands for toll-like receptors (TLR) are known to induce a variety of immune responses. Selective induction of desirable responses would be important for the treatment of individual diseases with various pathogenesis. For this purpose, we established six MAbs against the TLR4/MD-2 complex (UT MAbs) from TLR4(-/-) mice or MD-2(-/-) mice. Three MAbs (UT12, 18, and 22) induced NF-kappaB activation and production of pro-inflammatory cytokines, but the other three (UT15, 41, and 49) did not induce such cell responses. Unlike lipopolysaccharide (LPS), agonistic UT MAbs did not require serum components for the functions. UT41 and UT49 recognized TLR4 in the absence of MD-2. On the other hand, the other four MAbs reacted to the TLR4/MD-2 complex, but not to solo TLR4. Agonistic UT MAbs shared the epitopes, but non-agonistic UT15 reacted to distinct epitope on the complex. UT MAbs appear to be useful analyzing the molecular mechanism of TLR signaling and will contribute to the development of novel immunotherapies. |
| Databáze: | OpenAIRE |
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