A recombinant anti-erbB2, scFv-Fc-IL-2 fusion protein retains antigen specificity and cytokine function

Elevated erbB2 expression is detected in many in situ and invasive human ductal carcinomas. Anti-erbB2 antibody directed at the extracellular domain of erbB2 can result in an antitumor response in some patients with tumors overexpressing erbB2 oncoprotein. By combining interleukin 2 (IL-2) activitie...

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Published in:Biotechnology letters 2003-05, Vol.25 (10), p.815-819
Main Authors: Shi, Ming, Xie, Zhigang, Feng, Jiannan, Sun, Yingxun, Yu, Ming, Shen, Beifen, Guo, Ning
Format: Article
Language:English
Subjects:
Animals
Antigens
Biological and medical sciences
CHO Cells
Cricetinae
Cytokines - immunology
Fundamental and applied biological sciences. Psychology
Humans
Immunoglobulin Fragments - biosynthesis
Immunoglobulin Fragments - genetics
Immunoglobulin Fragments - immunology
Immunoglobulin Fragments - isolation & purification
Immunoglobulin G - genetics
Immunoglobulin G - metabolism
Immunotherapy
Interleukin-2 - genetics
Interleukin-2 - metabolism
Molecular weight
Pharmacokinetics
Proteins
Receptor, ErbB-2 - immunology
Recombinant Fusion Proteins - biosynthesis
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - immunology
Recombinant Fusion Proteins - isolation & purification
Sensitivity and Specificity
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container_issue 10
container_start_page 815
container_title Biotechnology letters
container_volume 25
creator Shi, Ming
Xie, Zhigang
Feng, Jiannan
Sun, Yingxun
Yu, Ming
Shen, Beifen
Guo, Ning
description Elevated erbB2 expression is detected in many in situ and invasive human ductal carcinomas. Anti-erbB2 antibody directed at the extracellular domain of erbB2 can result in an antitumor response in some patients with tumors overexpressing erbB2 oncoprotein. By combining interleukin 2 (IL-2) activities with a tumor specific antibody, immunotherapy of tumors might be more effective in the future. In this study, a fusion protein consisting of erbB2 single chain antibody (scFv), Fc fragment of human IgG1 and IL-2 was constructed. The molecular weight of fusion proteins is 66 kDa, only one third of whole antibody-IL-2 fusion protein or 44% whole Ig molecule. The fusion proteins retained the activities of both antigen binding and IL-2. The scFv-Fc-IL-2 fusion protein may have advantages over whole antibody-IL-2 fusion proteins, such as smaller molecule, better activity of penetration, more favorable pharmacokinetic properties.
doi_str_mv 10.1023/A:1023556523735
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Anti-erbB2 antibody directed at the extracellular domain of erbB2 can result in an antitumor response in some patients with tumors overexpressing erbB2 oncoprotein. By combining interleukin 2 (IL-2) activities with a tumor specific antibody, immunotherapy of tumors might be more effective in the future. In this study, a fusion protein consisting of erbB2 single chain antibody (scFv), Fc fragment of human IgG1 and IL-2 was constructed. The molecular weight of fusion proteins is 66 kDa, only one third of whole antibody-IL-2 fusion protein or 44% whole Ig molecule. The fusion proteins retained the activities of both antigen binding and IL-2. 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identifier ISSN: 0141-5492
ispartof Biotechnology letters, 2003-05, Vol.25 (10), p.815-819
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1573-6776
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source Springer Link
subjects Animals
Antigens
Biological and medical sciences
CHO Cells
Cricetinae
Cytokines - immunology
Fundamental and applied biological sciences. Psychology
Humans
Immunoglobulin Fragments - biosynthesis
Immunoglobulin Fragments - genetics
Immunoglobulin Fragments - immunology
Immunoglobulin Fragments - isolation & purification
Immunoglobulin G - genetics
Immunoglobulin G - metabolism
Immunotherapy
Interleukin-2 - genetics
Interleukin-2 - metabolism
Molecular weight
Pharmacokinetics
Proteins
Receptor, ErbB-2 - immunology
Recombinant Fusion Proteins - biosynthesis
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - immunology
Recombinant Fusion Proteins - isolation & purification
Sensitivity and Specificity
title A recombinant anti-erbB2, scFv-Fc-IL-2 fusion protein retains antigen specificity and cytokine function
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