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A recombinant single chain antibody interleukin-2 fusion protein.
Recombinant interleukin-2 (rIL-2) therapy has been shown to be of value in the treatment of some cases of melanoma and renal cell carcinoma. However its use can be limited by severe systemic toxicity. Targeting rIL-2 to the tumour should improve the anti-tumour immune response and decrease the syste...
Autores principales: | , , , |
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Formato: | Texto |
Lenguaje: | English |
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Nature Publishing Group
1993
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1968162/ https://www.ncbi.nlm.nih.gov/pubmed/8431359 |
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author | Savage, P. So, A. Spooner, R. A. Epenetos, A. A. |
author_facet | Savage, P. So, A. Spooner, R. A. Epenetos, A. A. |
author_sort | Savage, P. |
collection | PubMed |
description | Recombinant interleukin-2 (rIL-2) therapy has been shown to be of value in the treatment of some cases of melanoma and renal cell carcinoma. However its use can be limited by severe systemic toxicity. Targeting rIL-2 to the tumour should improve the anti-tumour immune response and decrease the systemic toxicity. With this aim we have employed recombinant DNA techniques to construct a single chain antibody interleukin-2 fusion protein (SCA-IL-2). The protein used in this model system comprises the variable domains of the anti-lysozyme antibody D1.3 fused to human IL-2. It has been expressed by secretion from Escherichia coli and the purified product possesses antigen binding specificity and retains the immunostimulatory activities of rIL-2. This approach can be taken to generate SCA-IL-2 proteins that bind to appropriate cellular antigens. In vivo administration of a tumour binding SCA-IL-2 should result in a localised high concentration of IL-2 in tumour tissues, maximising the anti-tumour immune response, whilst keeping systemic side effects to a minimum. IMAGES: |
format | Text |
id | pubmed-1968162 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1993 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-19681622009-09-10 A recombinant single chain antibody interleukin-2 fusion protein. Savage, P. So, A. Spooner, R. A. Epenetos, A. A. Br J Cancer Research Article Recombinant interleukin-2 (rIL-2) therapy has been shown to be of value in the treatment of some cases of melanoma and renal cell carcinoma. However its use can be limited by severe systemic toxicity. Targeting rIL-2 to the tumour should improve the anti-tumour immune response and decrease the systemic toxicity. With this aim we have employed recombinant DNA techniques to construct a single chain antibody interleukin-2 fusion protein (SCA-IL-2). The protein used in this model system comprises the variable domains of the anti-lysozyme antibody D1.3 fused to human IL-2. It has been expressed by secretion from Escherichia coli and the purified product possesses antigen binding specificity and retains the immunostimulatory activities of rIL-2. This approach can be taken to generate SCA-IL-2 proteins that bind to appropriate cellular antigens. In vivo administration of a tumour binding SCA-IL-2 should result in a localised high concentration of IL-2 in tumour tissues, maximising the anti-tumour immune response, whilst keeping systemic side effects to a minimum. IMAGES: Nature Publishing Group 1993-02 /pmc/articles/PMC1968162/ /pubmed/8431359 Text en https://creativecommons.org/licenses/by/4.0/This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit https://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Research Article Savage, P. So, A. Spooner, R. A. Epenetos, A. A. A recombinant single chain antibody interleukin-2 fusion protein. |
title | A recombinant single chain antibody interleukin-2 fusion protein. |
title_full | A recombinant single chain antibody interleukin-2 fusion protein. |
title_fullStr | A recombinant single chain antibody interleukin-2 fusion protein. |
title_full_unstemmed | A recombinant single chain antibody interleukin-2 fusion protein. |
title_short | A recombinant single chain antibody interleukin-2 fusion protein. |
title_sort | recombinant single chain antibody interleukin-2 fusion protein. |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1968162/ https://www.ncbi.nlm.nih.gov/pubmed/8431359 |
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