Autor: |
Zwirner, Jörg, Weissenhorn, Winfried, Karlsson, Lars, Becker, Andrea, Rieber, Ernst Peter, Riethmüller, Gert, Weiss, Elisabeth H., Peterson, Per A., Widera, Georg |
Jazyk: |
angličtina |
Rok vydání: |
1992 |
DOI: |
10.5282/ubm/epub.3042 |
Popis: |
composed of the a- and ß-chains of the MHC class I1I-E molecule fused to antibody V regions derivedfrom anti-human CD4 mAb MT310. Expression vectorswere constructed containing the functional,rearranged gene segments coding for the V regiondomains of the antibody H and L chains in place ofthe first domains of the complete structural genesof the I-E a- and ß-chains, respectively. Celltsr ansfectedwith both hybrid genes expressed a stableprotein product on the cell surface. The chimericmolecule exhibited the idiotype of the antibodyMT310 as shown by binding to the anti-idiotypicmAb 20-46. A protein of the anticipated molecularmass was immunoprecipitated witha nti-mouse IgGantiserum. Furthermore, human soluble CD4 didbind to thetr ansfected cell line, demonstrating thatthe chimeric protein possessed the binding capacityof the original mAb. Thus, the hybrid molecule retained:1) the properties of a MHC class I1 proteinwith regardt o correct chain assembly and transportto the cell surface: as well as 2) the Ag bindingcapacity of the antibody genes used. Thgee nerationof hybrid MHC class I1 molecules with highly specific,non-MHC-restricted bindingc apacities will beuseful for studying MHC class 11-mediated effectorfunctions such as selection of the T cell repertoirein thymus of transgenic mice. |
Databáze: |
OpenAIRE |
Externí odkaz: |
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