Anti‐CD30 (Ber‐H2) epitope requires structural elements as shown by mass spectroscopy and dual‐site associated kinetics
The Ber‐H2 mouse monoclonal antibody has been in use for 35 years for detecting the CD‐30 biomarker in a variety of lymphomas. Despite the wide use of this clone, we have not been successful in applying synthetic peptides derived from the published epitope sequence and affinity data toward the devel...
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| Veröffentlicht in: | Journal of molecular recognition 2023-06, Vol.36 (6), p.e3011-n/a |
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| creator | Warren, Phillip Daniel Smith, Margaret Helfrich |
| description | The Ber‐H2 mouse monoclonal antibody has been in use for 35 years for detecting the CD‐30 biomarker in a variety of lymphomas. Despite the wide use of this clone, we have not been successful in applying synthetic peptides derived from the published epitope sequence and affinity data toward the development of a new Ber‐H2‐based in vitro diagnostic reagent assay. We found that synthetic peptides based on the published epitope sequence do not function to inhibit antibody‐binding activity, thus indicating that the sequence is not the full epitope recognized by Ber‐H2. In this report, we used mass spectroscopic analysis of proteolyzed CD30 fragments capable of binding Ber‐H2 to identify additional regions within the epitope that participate in binding. Using surface plasmon resonance binding kinetic analyses and immuno‐histochemical peptide‐inhibition assays, we also demonstrate that the epitope sequence as originally reported is missing two key elements necessary for binding the Ber‐H2 antibody. |
| doi_str_mv | 10.1002/jmr.3011 |
| format | Article |
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Despite the wide use of this clone, we have not been successful in applying synthetic peptides derived from the published epitope sequence and affinity data toward the development of a new Ber‐H2‐based in vitro diagnostic reagent assay. We found that synthetic peptides based on the published epitope sequence do not function to inhibit antibody‐binding activity, thus indicating that the sequence is not the full epitope recognized by Ber‐H2. In this report, we used mass spectroscopic analysis of proteolyzed CD30 fragments capable of binding Ber‐H2 to identify additional regions within the epitope that participate in binding. Using surface plasmon resonance binding kinetic analyses and immuno‐histochemical peptide‐inhibition assays, we also demonstrate that the epitope sequence as originally reported is missing two key elements necessary for binding the Ber‐H2 antibody.</description><identifier>ISSN: 0952-3499</identifier><identifier>EISSN: 1099-1352</identifier><identifier>DOI: 10.1002/jmr.3011</identifier><identifier>PMID: 36971655</identifier><language>eng</language><publisher>England: Wiley Subscription Services, Inc</publisher><subject>Animals ; Antibodies, Monoclonal - metabolism ; Ber‐H2 clone ; Binding ; Biomarkers ; CD30 ; CD30 antigen ; Epitope Mapping ; Epitopes ; immunohistochemistry ; Ki-1 Antigen - analysis ; Ki-1 Antigen - chemistry ; Kinetics ; Lymphoma ; Mass Spectrometry ; Mass spectroscopy ; Mice ; Monoclonal antibodies ; Peptides ; Reagents ; Structural members ; Surface plasmon resonance ; Synthetic peptides</subject><ispartof>Journal of molecular recognition, 2023-06, Vol.36 (6), p.e3011-n/a</ispartof><rights>2023 Ventana Medical Systems. published by John Wiley & Sons Ltd.</rights><rights>2023 Ventana Medical Systems. 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Despite the wide use of this clone, we have not been successful in applying synthetic peptides derived from the published epitope sequence and affinity data toward the development of a new Ber‐H2‐based in vitro diagnostic reagent assay. We found that synthetic peptides based on the published epitope sequence do not function to inhibit antibody‐binding activity, thus indicating that the sequence is not the full epitope recognized by Ber‐H2. In this report, we used mass spectroscopic analysis of proteolyzed CD30 fragments capable of binding Ber‐H2 to identify additional regions within the epitope that participate in binding. Using surface plasmon resonance binding kinetic analyses and immuno‐histochemical peptide‐inhibition assays, we also demonstrate that the epitope sequence as originally reported is missing two key elements necessary for binding the Ber‐H2 antibody.</description><subject>Animals</subject><subject>Antibodies, Monoclonal - metabolism</subject><subject>Ber‐H2 clone</subject><subject>Binding</subject><subject>Biomarkers</subject><subject>CD30</subject><subject>CD30 antigen</subject><subject>Epitope Mapping</subject><subject>Epitopes</subject><subject>immunohistochemistry</subject><subject>Ki-1 Antigen - analysis</subject><subject>Ki-1 Antigen - chemistry</subject><subject>Kinetics</subject><subject>Lymphoma</subject><subject>Mass Spectrometry</subject><subject>Mass spectroscopy</subject><subject>Mice</subject><subject>Monoclonal antibodies</subject><subject>Peptides</subject><subject>Reagents</subject><subject>Structural members</subject><subject>Surface plasmon resonance</subject><subject>Synthetic peptides</subject><issn>0952-3499</issn><issn>1099-1352</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>24P</sourceid><sourceid>WIN</sourceid><sourceid>EIF</sourceid><recordid>eNp1kdtKHTEUhkNR6tYW-gQS6M32YmwOk5nkUnfrCUuhtNchk6yN2Z2TSQbZF4KP4DP6JMZDFQSvspL18bFWfoS-ULJPCWHfVl3Y54TSD2hGiVIF5YJtoBlRghW8VGoLbce4IiT3BPmItnilaloJMUPXB33ydze3i--c4PkhhFyfsD0Mo0_DCDjA5eQDRBxTmGyagmkxtNBBnyI2-fliuOpxs8adifk2gk1hiHYY19j0DrvJtNkYfYJMx8F6k8Dhf76H5G38hDaXpo3w-fncQX-PfvxZnBTnv45PFwfnheVlSQvrjGyMkYRLVwuooWRKLl1VNY0AkMqxSkhF6ooIapYlM8pyRmpeW0qdtJzvoPmTdwzD5QQx6c5HC21rehimqFmtaJ0_R9GMfn2DroYp9Hk6zSRltOSEyVehzdvGAEs9Bt-ZsNaU6IdIdI5EP0SS0d1n4dR04F7A_xlkoHgCrnwL63dF-uzn70fhPQtil7g</recordid><startdate>202306</startdate><enddate>202306</enddate><creator>Warren, Phillip Daniel</creator><creator>Smith, Margaret Helfrich</creator><general>Wiley Subscription Services, Inc</general><scope>24P</scope><scope>WIN</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QF</scope><scope>7QO</scope><scope>7QP</scope><scope>7QQ</scope><scope>7SE</scope><scope>7SR</scope><scope>7TA</scope><scope>7TK</scope><scope>7TM</scope><scope>8BQ</scope><scope>8FD</scope><scope>F28</scope><scope>FR3</scope><scope>H8G</scope><scope>JG9</scope><scope>P64</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-9510-0789</orcidid></search><sort><creationdate>202306</creationdate><title>Anti‐CD30 (Ber‐H2) epitope requires structural elements as shown by mass spectroscopy and dual‐site associated kinetics</title><author>Warren, Phillip Daniel ; Smith, Margaret Helfrich</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3441-cda8baa8038d75e7e4298fd66bb5ee89d26589076051af42a9c320737c11d8c33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Animals</topic><topic>Antibodies, Monoclonal - metabolism</topic><topic>Ber‐H2 clone</topic><topic>Binding</topic><topic>Biomarkers</topic><topic>CD30</topic><topic>CD30 antigen</topic><topic>Epitope Mapping</topic><topic>Epitopes</topic><topic>immunohistochemistry</topic><topic>Ki-1 Antigen - analysis</topic><topic>Ki-1 Antigen - chemistry</topic><topic>Kinetics</topic><topic>Lymphoma</topic><topic>Mass Spectrometry</topic><topic>Mass spectroscopy</topic><topic>Mice</topic><topic>Monoclonal antibodies</topic><topic>Peptides</topic><topic>Reagents</topic><topic>Structural members</topic><topic>Surface plasmon resonance</topic><topic>Synthetic peptides</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Warren, Phillip Daniel</creatorcontrib><creatorcontrib>Smith, Margaret Helfrich</creatorcontrib><collection>Wiley-Blackwell Open Access Titles(OpenAccess)</collection><collection>Wiley Online Library Free Content</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Aluminium Industry Abstracts</collection><collection>Biotechnology Research Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Ceramic Abstracts</collection><collection>Corrosion Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Materials Business File</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Engineering Research Database</collection><collection>Copper Technical Reference Library</collection><collection>Materials Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of molecular recognition</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Warren, Phillip Daniel</au><au>Smith, Margaret Helfrich</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Anti‐CD30 (Ber‐H2) epitope requires structural elements as shown by mass spectroscopy and dual‐site associated kinetics</atitle><jtitle>Journal of molecular recognition</jtitle><addtitle>J Mol Recognit</addtitle><date>2023-06</date><risdate>2023</risdate><volume>36</volume><issue>6</issue><spage>e3011</spage><epage>n/a</epage><pages>e3011-n/a</pages><issn>0952-3499</issn><eissn>1099-1352</eissn><abstract>The Ber‐H2 mouse monoclonal antibody has been in use for 35 years for detecting the CD‐30 biomarker in a variety of lymphomas. Despite the wide use of this clone, we have not been successful in applying synthetic peptides derived from the published epitope sequence and affinity data toward the development of a new Ber‐H2‐based in vitro diagnostic reagent assay. We found that synthetic peptides based on the published epitope sequence do not function to inhibit antibody‐binding activity, thus indicating that the sequence is not the full epitope recognized by Ber‐H2. In this report, we used mass spectroscopic analysis of proteolyzed CD30 fragments capable of binding Ber‐H2 to identify additional regions within the epitope that participate in binding. 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| subjects | Animals Antibodies, Monoclonal - metabolism Ber‐H2 clone Binding Biomarkers CD30 CD30 antigen Epitope Mapping Epitopes immunohistochemistry Ki-1 Antigen - analysis Ki-1 Antigen - chemistry Kinetics Lymphoma Mass Spectrometry Mass spectroscopy Mice Monoclonal antibodies Peptides Reagents Structural members Surface plasmon resonance Synthetic peptides |
| title | Anti‐CD30 (Ber‐H2) epitope requires structural elements as shown by mass spectroscopy and dual‐site associated kinetics |
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