Structural and functional evaluation of single-chain Fv antibody HyC1 recognizing the residual native structure of hen egg lysozyme
Evaluation of the molecular mechanisms by which an antibody recognizes a specific antigen could help in better understanding of the protein recognition mechanisms. We previously showed that anti-hen egg lysozyme (HEL) monoclonal antibody, HyC1, recognized the structural and hydrodynamic change in HE...
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| Veröffentlicht in: | Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2020-02, Vol.84 (2), p.358-364 |
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| container_title | Bioscience, biotechnology, and biochemistry |
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| creator | Yamaoka, Takanori Kamatari, Yuji O. Maruno, Takahiro Kobayashi, Yuji Oda, Masayuki |
| description | Evaluation of the molecular mechanisms by which an antibody recognizes a specific antigen could help in better understanding of the protein recognition mechanisms. We previously showed that anti-hen egg lysozyme (HEL) monoclonal antibody, HyC1, recognized the structural and hydrodynamic change in HEL. Here, we generated HyC1 single-chain Fv (scFv), and characterized it using different structural and biophysical methods. Similar to HyC1 monoclonal antibody, HyC1 scFv could recognize native HEL from carboxymethylated Cys6 and Cys127 HEL (CM
6,127
-HEL). Comparison of the binding thermodynamics of HyC1 scFv between HEL and CM
6,127
-HEL showed that the binding enthalpy change was different, while the binding entropy was remained unchanged. The results indicated that the fluctuation of the residual native structure in both HEL and CM
6,127
-HEL was similar. The NMR experiments for
15
N-labeled HyC1 scFv indicated that the flexibility of HyC1 scFv decreased upon the binding to HEL.
HyC1 single-chain Fv (scFv) could recognize native HEL from carboxymethylated Cys6 and Cys127 HEL (CM
6,127
-HEL). |
| doi_str_mv | 10.1080/09168451.2019.1683441 |
| format | Article |
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6,127
-HEL). Comparison of the binding thermodynamics of HyC1 scFv between HEL and CM
6,127
-HEL showed that the binding enthalpy change was different, while the binding entropy was remained unchanged. The results indicated that the fluctuation of the residual native structure in both HEL and CM
6,127
-HEL was similar. The NMR experiments for
15
N-labeled HyC1 scFv indicated that the flexibility of HyC1 scFv decreased upon the binding to HEL.
HyC1 single-chain Fv (scFv) could recognize native HEL from carboxymethylated Cys6 and Cys127 HEL (CM
6,127
-HEL).</description><identifier>ISSN: 0916-8451</identifier><identifier>EISSN: 1347-6947</identifier><identifier>DOI: 10.1080/09168451.2019.1683441</identifier><identifier>PMID: 31662101</identifier><language>eng</language><publisher>England: Taylor & Francis</publisher><subject>Animals ; Antigen binding ; Calorimetry ; isothermal titration calorimetry ; Magnetic Resonance Spectroscopy ; Muramidase - chemistry ; Muramidase - immunology ; NMR ; Protein Conformation ; refolding ; Single-Chain Antibodies - chemistry ; Single-Chain Antibodies - immunology ; Surface Plasmon Resonance ; Thermodynamics</subject><ispartof>Bioscience, biotechnology, and biochemistry, 2020-02, Vol.84 (2), p.358-364</ispartof><rights>2019 Japan Society for Bioscience, Biotechnology, and Agrochemistry 2019</rights><rights>2020 Japan Society for Bioscience, Biotechnology, and Agrochemistry 2020</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c544t-4841e83918d660ac0dfaaf96a9a2da5a137374d41a86d69a406ab31305628f833</citedby><cites>FETCH-LOGICAL-c544t-4841e83918d660ac0dfaaf96a9a2da5a137374d41a86d69a406ab31305628f833</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27905,27906</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31662101$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yamaoka, Takanori</creatorcontrib><creatorcontrib>Kamatari, Yuji O.</creatorcontrib><creatorcontrib>Maruno, Takahiro</creatorcontrib><creatorcontrib>Kobayashi, Yuji</creatorcontrib><creatorcontrib>Oda, Masayuki</creatorcontrib><title>Structural and functional evaluation of single-chain Fv antibody HyC1 recognizing the residual native structure of hen egg lysozyme</title><title>Bioscience, biotechnology, and biochemistry</title><addtitle>Biosci Biotechnol Biochem</addtitle><description>Evaluation of the molecular mechanisms by which an antibody recognizes a specific antigen could help in better understanding of the protein recognition mechanisms. We previously showed that anti-hen egg lysozyme (HEL) monoclonal antibody, HyC1, recognized the structural and hydrodynamic change in HEL. Here, we generated HyC1 single-chain Fv (scFv), and characterized it using different structural and biophysical methods. Similar to HyC1 monoclonal antibody, HyC1 scFv could recognize native HEL from carboxymethylated Cys6 and Cys127 HEL (CM
6,127
-HEL). Comparison of the binding thermodynamics of HyC1 scFv between HEL and CM
6,127
-HEL showed that the binding enthalpy change was different, while the binding entropy was remained unchanged. The results indicated that the fluctuation of the residual native structure in both HEL and CM
6,127
-HEL was similar. The NMR experiments for
15
N-labeled HyC1 scFv indicated that the flexibility of HyC1 scFv decreased upon the binding to HEL.
HyC1 single-chain Fv (scFv) could recognize native HEL from carboxymethylated Cys6 and Cys127 HEL (CM
6,127
-HEL).</description><subject>Animals</subject><subject>Antigen binding</subject><subject>Calorimetry</subject><subject>isothermal titration calorimetry</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Muramidase - chemistry</subject><subject>Muramidase - immunology</subject><subject>NMR</subject><subject>Protein Conformation</subject><subject>refolding</subject><subject>Single-Chain Antibodies - chemistry</subject><subject>Single-Chain Antibodies - immunology</subject><subject>Surface Plasmon Resonance</subject><subject>Thermodynamics</subject><issn>0916-8451</issn><issn>1347-6947</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkE2P0zAQhi0EYsvCTwD5yCXFEzuucwNVLLvSShyAczT1R2uU2MVOirJX_jiO2uW44mTP6HmfkV5C3gJbA1PsA2tBKtHAumbQrsufCwHPyAq42FSyFZvnZLUw1QJdkVc5_2SsLBp4Sa44SFkDgxX5821Mkx6nhD3FYKibgh59DGW0J-wnXAYaHc0-7Htb6QP6QG9OBR79LpqZ3s5boMnquA_-oUB0PNgyZ2-mIglFcLI0X67YRXWwgdr9nvZzjg_zYF-TFw77bN9c3mvy4-bz9-1tdf_1y932032lGyHGSigBVvEWlJGSoWbGIbpWYou1wQaBb_hGGAGopJEtCiZxx4GzRtbKKc6vyfuz95jir8nmsRt81rbvMdg45a7mwKRULSxoc0Z1ijkn67pj8gOmuQPWLf13j_13S__dpf-Se3c5Me0Ga_6lHgsvADsDcTr-t_PjOeKDi2nA3zH1phtx7mNyCYP2ufifVPwFRuuj0Q</recordid><startdate>20200201</startdate><enddate>20200201</enddate><creator>Yamaoka, Takanori</creator><creator>Kamatari, Yuji O.</creator><creator>Maruno, Takahiro</creator><creator>Kobayashi, Yuji</creator><creator>Oda, Masayuki</creator><general>Taylor & Francis</general><general>Oxford University Press</general><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>7X8</scope></search><sort><creationdate>20200201</creationdate><title>Structural and functional evaluation of single-chain Fv antibody HyC1 recognizing the residual native structure of hen egg lysozyme</title><author>Yamaoka, Takanori ; Kamatari, Yuji O. ; Maruno, Takahiro ; Kobayashi, Yuji ; Oda, Masayuki</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c544t-4841e83918d660ac0dfaaf96a9a2da5a137374d41a86d69a406ab31305628f833</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Animals</topic><topic>Antigen binding</topic><topic>Calorimetry</topic><topic>isothermal titration calorimetry</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Muramidase - chemistry</topic><topic>Muramidase - immunology</topic><topic>NMR</topic><topic>Protein Conformation</topic><topic>refolding</topic><topic>Single-Chain Antibodies - chemistry</topic><topic>Single-Chain Antibodies - immunology</topic><topic>Surface Plasmon Resonance</topic><topic>Thermodynamics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yamaoka, Takanori</creatorcontrib><creatorcontrib>Kamatari, Yuji O.</creatorcontrib><creatorcontrib>Maruno, Takahiro</creatorcontrib><creatorcontrib>Kobayashi, Yuji</creatorcontrib><creatorcontrib>Oda, Masayuki</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Bioscience, biotechnology, and biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yamaoka, Takanori</au><au>Kamatari, Yuji O.</au><au>Maruno, Takahiro</au><au>Kobayashi, Yuji</au><au>Oda, Masayuki</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural and functional evaluation of single-chain Fv antibody HyC1 recognizing the residual native structure of hen egg lysozyme</atitle><jtitle>Bioscience, biotechnology, and biochemistry</jtitle><addtitle>Biosci Biotechnol Biochem</addtitle><date>2020-02-01</date><risdate>2020</risdate><volume>84</volume><issue>2</issue><spage>358</spage><epage>364</epage><pages>358-364</pages><issn>0916-8451</issn><eissn>1347-6947</eissn><abstract>Evaluation of the molecular mechanisms by which an antibody recognizes a specific antigen could help in better understanding of the protein recognition mechanisms. We previously showed that anti-hen egg lysozyme (HEL) monoclonal antibody, HyC1, recognized the structural and hydrodynamic change in HEL. Here, we generated HyC1 single-chain Fv (scFv), and characterized it using different structural and biophysical methods. Similar to HyC1 monoclonal antibody, HyC1 scFv could recognize native HEL from carboxymethylated Cys6 and Cys127 HEL (CM
6,127
-HEL). Comparison of the binding thermodynamics of HyC1 scFv between HEL and CM
6,127
-HEL showed that the binding enthalpy change was different, while the binding entropy was remained unchanged. The results indicated that the fluctuation of the residual native structure in both HEL and CM
6,127
-HEL was similar. The NMR experiments for
15
N-labeled HyC1 scFv indicated that the flexibility of HyC1 scFv decreased upon the binding to HEL.
HyC1 single-chain Fv (scFv) could recognize native HEL from carboxymethylated Cys6 and Cys127 HEL (CM
6,127
-HEL).</abstract><cop>England</cop><pub>Taylor & Francis</pub><pmid>31662101</pmid><doi>10.1080/09168451.2019.1683441</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| language | eng |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Oxford University Press Journals All Titles (1996-Current); Open Access Titles of Japan |
| subjects | Animals Antigen binding Calorimetry isothermal titration calorimetry Magnetic Resonance Spectroscopy Muramidase - chemistry Muramidase - immunology NMR Protein Conformation refolding Single-Chain Antibodies - chemistry Single-Chain Antibodies - immunology Surface Plasmon Resonance Thermodynamics |
| title | Structural and functional evaluation of single-chain Fv antibody HyC1 recognizing the residual native structure of hen egg lysozyme |
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