A New Antibody Recognizing the vIII Mutation of Human Epidermal Growth Factor Receptor
The epidermal growth factor receptor (EGFR) gene is frequently amplified and the receptor overexpressed in different types of human tumors. Furthermore, genomic rearrangements can cause expression of modified receptors, as one frequently occurring truncated form, EGFRvIII. This mutated receptor has...
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| Veröffentlicht in: | Tumor biology 2002-03, Vol.23 (2), p.61-69 |
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| creator | Öhman, Linda Gedda, Lars Hesselager, Göran Larsson, Rolf Nister, Monica Stigbrand, Torgny Wester, Kenneth Carlsson, Jörgen |
| description | The epidermal growth factor receptor (EGFR) gene is frequently amplified and the receptor overexpressed in different types of human tumors. Furthermore, genomic rearrangements can cause expression of modified receptors, as one frequently occurring truncated form, EGFRvIII. This mutated receptor has previously been described and is formed by a 267-amino acid in-frame deletion and an insertion of a glycine in the fusion junction of the extracellular domain. EGFRvIII is a tumor-specific marker and therefore of interest for diagnostic and therapeutic applications. In this study we report on a new monoclonal antibody (Ua30:2) directed to the mutation site of EGFRvIII. The antibody was generated by immunization of mice with a synthetic peptide corresponding to the mutated sequence of the receptor. The affinity of Ua30:2 was found to be high [K d = 45 nM (Biacore) and 80 nM (saturation analysis)]. Immunohistochemistry in tissue sections from human gliomas demonstrated a similar expression pattern for Ua30:2 as for the recently characterized antibodies L8A4 and DH8.3. The antibody binding was EGFRvIII specific with no measurable cross-reactivity to the wild-type receptor, wtEGFR, as analyzed both with displacement analysis, Western blots and immunohistochemistry. The new antibody is a candidate for radioimmunotargeting aiming at diagnostic and therapeutic applications. |
| doi_str_mv | 10.1159/000059704 |
| format | Article |
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Furthermore, genomic rearrangements can cause expression of modified receptors, as one frequently occurring truncated form, EGFRvIII. This mutated receptor has previously been described and is formed by a 267-amino acid in-frame deletion and an insertion of a glycine in the fusion junction of the extracellular domain. EGFRvIII is a tumor-specific marker and therefore of interest for diagnostic and therapeutic applications. In this study we report on a new monoclonal antibody (Ua30:2) directed to the mutation site of EGFRvIII. The antibody was generated by immunization of mice with a synthetic peptide corresponding to the mutated sequence of the receptor. The affinity of Ua30:2 was found to be high [K d = 45 nM (Biacore) and 80 nM (saturation analysis)]. Immunohistochemistry in tissue sections from human gliomas demonstrated a similar expression pattern for Ua30:2 as for the recently characterized antibodies L8A4 and DH8.3. The antibody binding was EGFRvIII specific with no measurable cross-reactivity to the wild-type receptor, wtEGFR, as analyzed both with displacement analysis, Western blots and immunohistochemistry. The new antibody is a candidate for radioimmunotargeting aiming at diagnostic and therapeutic applications.</description><identifier>ISSN: 1010-4283</identifier><identifier>EISSN: 1423-0380</identifier><identifier>DOI: 10.1159/000059704</identifier><identifier>PMID: 12065843</identifier><identifier>CODEN: OBIMD4</identifier><language>eng</language><publisher>Basel, Switzerland: Karger</publisher><subject>Amino Acid Sequence ; Animals ; Antibodies, Monoclonal - immunology ; Antibody Affinity ; Antigen-Antibody Reactions ; Biological and medical sciences ; Blotting, Western ; Brain Neoplasms - chemistry ; Female ; Glioblastoma - chemistry ; Heparin - pharmacology ; Humans ; Immunoenzyme Techniques ; Iodine Radioisotopes ; Medical sciences ; Medicin och hälsovetenskap ; Mice ; Mice, Inbred BALB C ; Molecular Sequence Data ; Neoplasm Proteins - analysis ; Neoplasm Proteins - chemistry ; Neoplasm Proteins - genetics ; Neoplasm Proteins - immunology ; Peptide Fragments - chemical synthesis ; Peptide Fragments - immunology ; Radiation therapy and radiosensitizing agent ; Radioimmunodetection ; Radioimmunotherapy ; Receptor, Epidermal Growth Factor - analysis ; Receptor, Epidermal Growth Factor - chemistry ; Receptor, Epidermal Growth Factor - genetics ; Receptor, Epidermal Growth Factor - immunology ; Research Article ; Treatment with physical agents ; Treatment. General aspects ; Tumors</subject><ispartof>Tumor biology, 2002-03, Vol.23 (2), p.61-69</ispartof><rights>2002 S. Karger AG, Basel</rights><rights>2002 INIST-CNRS</rights><rights>Copyright 2002 S. Karger AG, Basel</rights><rights>Copyright (c) 2002 S. Karger AG, Basel</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c503t-9854aee0a2d4a4227fd24bedf909c1f9f69f8ecac3bffe65f838f1647220cab03</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,315,781,785,886,2430,27929,27930</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=13755025$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12065843$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttp://kipublications.ki.se/Default.aspx?queryparsed=id:18447977$$DView record from Swedish Publication Index$$Hfree_for_read</backlink></links><search><creatorcontrib>Öhman, Linda</creatorcontrib><creatorcontrib>Gedda, Lars</creatorcontrib><creatorcontrib>Hesselager, Göran</creatorcontrib><creatorcontrib>Larsson, Rolf</creatorcontrib><creatorcontrib>Nister, Monica</creatorcontrib><creatorcontrib>Stigbrand, Torgny</creatorcontrib><creatorcontrib>Wester, Kenneth</creatorcontrib><creatorcontrib>Carlsson, Jörgen</creatorcontrib><title>A New Antibody Recognizing the vIII Mutation of Human Epidermal Growth Factor Receptor</title><title>Tumor biology</title><addtitle>Tumor Biol</addtitle><description>The epidermal growth factor receptor (EGFR) gene is frequently amplified and the receptor overexpressed in different types of human tumors. Furthermore, genomic rearrangements can cause expression of modified receptors, as one frequently occurring truncated form, EGFRvIII. This mutated receptor has previously been described and is formed by a 267-amino acid in-frame deletion and an insertion of a glycine in the fusion junction of the extracellular domain. EGFRvIII is a tumor-specific marker and therefore of interest for diagnostic and therapeutic applications. In this study we report on a new monoclonal antibody (Ua30:2) directed to the mutation site of EGFRvIII. The antibody was generated by immunization of mice with a synthetic peptide corresponding to the mutated sequence of the receptor. The affinity of Ua30:2 was found to be high [K d = 45 nM (Biacore) and 80 nM (saturation analysis)]. Immunohistochemistry in tissue sections from human gliomas demonstrated a similar expression pattern for Ua30:2 as for the recently characterized antibodies L8A4 and DH8.3. The antibody binding was EGFRvIII specific with no measurable cross-reactivity to the wild-type receptor, wtEGFR, as analyzed both with displacement analysis, Western blots and immunohistochemistry. The new antibody is a candidate for radioimmunotargeting aiming at diagnostic and therapeutic applications.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antibodies, Monoclonal - immunology</subject><subject>Antibody Affinity</subject><subject>Antigen-Antibody Reactions</subject><subject>Biological and medical sciences</subject><subject>Blotting, Western</subject><subject>Brain Neoplasms - chemistry</subject><subject>Female</subject><subject>Glioblastoma - chemistry</subject><subject>Heparin - pharmacology</subject><subject>Humans</subject><subject>Immunoenzyme Techniques</subject><subject>Iodine Radioisotopes</subject><subject>Medical sciences</subject><subject>Medicin och hälsovetenskap</subject><subject>Mice</subject><subject>Mice, Inbred BALB C</subject><subject>Molecular Sequence Data</subject><subject>Neoplasm Proteins - analysis</subject><subject>Neoplasm Proteins - chemistry</subject><subject>Neoplasm Proteins - genetics</subject><subject>Neoplasm Proteins - immunology</subject><subject>Peptide Fragments - chemical synthesis</subject><subject>Peptide Fragments - immunology</subject><subject>Radiation therapy and radiosensitizing agent</subject><subject>Radioimmunodetection</subject><subject>Radioimmunotherapy</subject><subject>Receptor, Epidermal Growth Factor - analysis</subject><subject>Receptor, Epidermal Growth Factor - chemistry</subject><subject>Receptor, Epidermal Growth Factor - genetics</subject><subject>Receptor, Epidermal Growth Factor - immunology</subject><subject>Research Article</subject><subject>Treatment with physical agents</subject><subject>Treatment. 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Furthermore, genomic rearrangements can cause expression of modified receptors, as one frequently occurring truncated form, EGFRvIII. This mutated receptor has previously been described and is formed by a 267-amino acid in-frame deletion and an insertion of a glycine in the fusion junction of the extracellular domain. EGFRvIII is a tumor-specific marker and therefore of interest for diagnostic and therapeutic applications. In this study we report on a new monoclonal antibody (Ua30:2) directed to the mutation site of EGFRvIII. The antibody was generated by immunization of mice with a synthetic peptide corresponding to the mutated sequence of the receptor. The affinity of Ua30:2 was found to be high [K d = 45 nM (Biacore) and 80 nM (saturation analysis)]. Immunohistochemistry in tissue sections from human gliomas demonstrated a similar expression pattern for Ua30:2 as for the recently characterized antibodies L8A4 and DH8.3. The antibody binding was EGFRvIII specific with no measurable cross-reactivity to the wild-type receptor, wtEGFR, as analyzed both with displacement analysis, Western blots and immunohistochemistry. The new antibody is a candidate for radioimmunotargeting aiming at diagnostic and therapeutic applications.</abstract><cop>Basel, Switzerland</cop><pub>Karger</pub><pmid>12065843</pmid><doi>10.1159/000059704</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Tumor biology, 2002-03, Vol.23 (2), p.61-69 |
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| subjects | Amino Acid Sequence Animals Antibodies, Monoclonal - immunology Antibody Affinity Antigen-Antibody Reactions Biological and medical sciences Blotting, Western Brain Neoplasms - chemistry Female Glioblastoma - chemistry Heparin - pharmacology Humans Immunoenzyme Techniques Iodine Radioisotopes Medical sciences Medicin och hälsovetenskap Mice Mice, Inbred BALB C Molecular Sequence Data Neoplasm Proteins - analysis Neoplasm Proteins - chemistry Neoplasm Proteins - genetics Neoplasm Proteins - immunology Peptide Fragments - chemical synthesis Peptide Fragments - immunology Radiation therapy and radiosensitizing agent Radioimmunodetection Radioimmunotherapy Receptor, Epidermal Growth Factor - analysis Receptor, Epidermal Growth Factor - chemistry Receptor, Epidermal Growth Factor - genetics Receptor, Epidermal Growth Factor - immunology Research Article Treatment with physical agents Treatment. General aspects Tumors |
| title | A New Antibody Recognizing the vIII Mutation of Human Epidermal Growth Factor Receptor |
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