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Phage Display Based Cloning of Proteins Interacting with the Cytoplasmic Tail of Membrane Immunoglobulins
The reduced quantity and quality of serum immunoglobulins (sIgs) in mutant mice expressing truncated cytoplasmic tails of IgE and IgG1 indicate an active role for the cytoplasmic domains of mIgG1 and mIgE. We used phage display technology to identify candidate proteins able to interact with the cyto...
Autores principales: | , , , , , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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Hindawi Publishing Corporation
2002
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2276102/ https://www.ncbi.nlm.nih.gov/pubmed/12885153 http://dx.doi.org/10.1080/1044667031000137584 |
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author | Geisberger, Roland Prlic, Martin Achatz-Straussberger, Gertrude Oberndorfer, Iris Luger, Elke Lamers, Marinus Crameri, Reto Appenzeller, Ulrich Wienands, Jürgen Breitenbach, Michael Ferreira, Fatima Achatz, Gernot |
author_facet | Geisberger, Roland Prlic, Martin Achatz-Straussberger, Gertrude Oberndorfer, Iris Luger, Elke Lamers, Marinus Crameri, Reto Appenzeller, Ulrich Wienands, Jürgen Breitenbach, Michael Ferreira, Fatima Achatz, Gernot |
author_sort | Geisberger, Roland |
collection | PubMed |
description | The reduced quantity and quality of serum immunoglobulins (sIgs) in mutant mice expressing truncated cytoplasmic tails of IgE and IgG1 indicate an active role for the cytoplasmic domains of mIgG1 and mIgE. We used phage display technology to identify candidate proteins able to interact with the cytoplasmic tail of mIgE. Using a murine cDNA B cell library displayed on the surface of phage as prey and the 28 amino acid long cytoplasmic tail of IgE as bait, we isolated phage encoding the murine hematopoietic progenitor kinase 1 (HPK1). Surface plasmon resonance analysis measurements confirmed affinity of HPK1 to the mIgE cytoplasmic tail and revealed association to other immunoglobulin isotypes as well. Immunoprecipitation experiments, using lysates from two B cell lines expressing nitrophenyl (NP) specific mIgE molecules showed co-precipitation of IgE and HPK1. The interaction of HPK1 with the cytoplasmic domains of membrane immunoglobulins indicate an active role of the tails as part of an isotype specific signal transduction, independent from the Igα/Igβ heterodimers, and may represent a missing link to upstream regulatory elements of HPK1 activation. |
format | Text |
id | pubmed-2276102 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2002 |
publisher | Hindawi Publishing Corporation |
record_format | MEDLINE/PubMed |
spelling | pubmed-22761022008-03-31 Phage Display Based Cloning of Proteins Interacting with the Cytoplasmic Tail of Membrane Immunoglobulins Geisberger, Roland Prlic, Martin Achatz-Straussberger, Gertrude Oberndorfer, Iris Luger, Elke Lamers, Marinus Crameri, Reto Appenzeller, Ulrich Wienands, Jürgen Breitenbach, Michael Ferreira, Fatima Achatz, Gernot Dev Immunol Research Article The reduced quantity and quality of serum immunoglobulins (sIgs) in mutant mice expressing truncated cytoplasmic tails of IgE and IgG1 indicate an active role for the cytoplasmic domains of mIgG1 and mIgE. We used phage display technology to identify candidate proteins able to interact with the cytoplasmic tail of mIgE. Using a murine cDNA B cell library displayed on the surface of phage as prey and the 28 amino acid long cytoplasmic tail of IgE as bait, we isolated phage encoding the murine hematopoietic progenitor kinase 1 (HPK1). Surface plasmon resonance analysis measurements confirmed affinity of HPK1 to the mIgE cytoplasmic tail and revealed association to other immunoglobulin isotypes as well. Immunoprecipitation experiments, using lysates from two B cell lines expressing nitrophenyl (NP) specific mIgE molecules showed co-precipitation of IgE and HPK1. The interaction of HPK1 with the cytoplasmic domains of membrane immunoglobulins indicate an active role of the tails as part of an isotype specific signal transduction, independent from the Igα/Igβ heterodimers, and may represent a missing link to upstream regulatory elements of HPK1 activation. Hindawi Publishing Corporation 2002-09 /pmc/articles/PMC2276102/ /pubmed/12885153 http://dx.doi.org/10.1080/1044667031000137584 Text en Copyright © 2002 Hindawi Publishing Corporation. http://creativecommons.org/licenses/by/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Geisberger, Roland Prlic, Martin Achatz-Straussberger, Gertrude Oberndorfer, Iris Luger, Elke Lamers, Marinus Crameri, Reto Appenzeller, Ulrich Wienands, Jürgen Breitenbach, Michael Ferreira, Fatima Achatz, Gernot Phage Display Based Cloning of Proteins Interacting with the Cytoplasmic Tail of Membrane Immunoglobulins |
title | Phage Display Based Cloning of Proteins Interacting with the Cytoplasmic Tail of Membrane Immunoglobulins |
title_full | Phage Display Based Cloning of Proteins Interacting with the Cytoplasmic Tail of Membrane Immunoglobulins |
title_fullStr | Phage Display Based Cloning of Proteins Interacting with the Cytoplasmic Tail of Membrane Immunoglobulins |
title_full_unstemmed | Phage Display Based Cloning of Proteins Interacting with the Cytoplasmic Tail of Membrane Immunoglobulins |
title_short | Phage Display Based Cloning of Proteins Interacting with the Cytoplasmic Tail of Membrane Immunoglobulins |
title_sort | phage display based cloning of proteins interacting with the cytoplasmic tail of membrane immunoglobulins |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2276102/ https://www.ncbi.nlm.nih.gov/pubmed/12885153 http://dx.doi.org/10.1080/1044667031000137584 |
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