DNA hydrolysis by monoclonal autoantibody BV 04-01
Monoclonal anti-DNA autoantibody BV 04-01 catalyzed hydrolysis of DNA in the presence of Mg2+. Catalysis was associated with BV 04-01 IgG, Fab, and single-chain-antibody (SCA) proteins. Cleavage of both ss and dsDNA was observed with efficient hydrolysis of the C-rich region of A7C7ATATAGCGCGT2, as...
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| Veröffentlicht in: | Applied biochemistry and biotechnology 2000-01, Vol.83 (1-3), p.95-105 |
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| creator | Rodkey, L S Gololobov, G Rumbley, C A Rumbley, J Schourov, D V Makarevich, O I Gabibov, A G Voss, Jr, E W |
| description | Monoclonal anti-DNA autoantibody BV 04-01 catalyzed hydrolysis of DNA in the presence of Mg2+. Catalysis was associated with BV 04-01 IgG, Fab, and single-chain-antibody (SCA) proteins. Cleavage of both ss and dsDNA was observed with efficient hydrolysis of the C-rich region of A7C7ATATAGCGCGT2, as well as a preference for cleaving within CG-rich regions of dsDNA. Data on specificity of ssDNA hydrolysis and kinetic data obtained from wild-type SCA, and two SCA mutants were used to model the catalytically active antibody site using the previously resolved X-ray structure of BV 04-01. The resulting model suggested that the target phosphodiester bond is activated by induction of conformational strain. In addition, the antibody-DNA complex contained a Mg2+ coordination site composed of the L32Tyr and L27dHis side chains and a DNA 3'-phosphodiester group. Induction of strain along with the metal coordination could be part of the mechanism by which this antibody catalyzes DNA hydrolysis. Sequence data for BV 04-01 V(H) and V(L) genes suggested that the proposed catalytic-antibody active site was germline-encoded. This observation suggests that catalytic activity might represent an important-rarely examined-function for some antibody molecules. |
| doi_str_mv | 10.1385/abab:83:1-3:95 |
| format | Article |
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Catalysis was associated with BV 04-01 IgG, Fab, and single-chain-antibody (SCA) proteins. Cleavage of both ss and dsDNA was observed with efficient hydrolysis of the C-rich region of A7C7ATATAGCGCGT2, as well as a preference for cleaving within CG-rich regions of dsDNA. Data on specificity of ssDNA hydrolysis and kinetic data obtained from wild-type SCA, and two SCA mutants were used to model the catalytically active antibody site using the previously resolved X-ray structure of BV 04-01. The resulting model suggested that the target phosphodiester bond is activated by induction of conformational strain. In addition, the antibody-DNA complex contained a Mg2+ coordination site composed of the L32Tyr and L27dHis side chains and a DNA 3'-phosphodiester group. Induction of strain along with the metal coordination could be part of the mechanism by which this antibody catalyzes DNA hydrolysis. Sequence data for BV 04-01 V(H) and V(L) genes suggested that the proposed catalytic-antibody active site was germline-encoded. This observation suggests that catalytic activity might represent an important-rarely examined-function for some antibody molecules.</description><identifier>ISSN: 0273-2289</identifier><identifier>EISSN: 0273-2289</identifier><identifier>EISSN: 1559-0291</identifier><identifier>DOI: 10.1385/abab:83:1-3:95</identifier><identifier>PMID: 10826952</identifier><language>eng</language><publisher>United States: Springer Nature B.V</publisher><subject>Animals ; Antibodies ; Antibodies, Antinuclear - chemistry ; Antibodies, Antinuclear - genetics ; Antibodies, Antinuclear - metabolism ; Antibodies, Catalytic - chemistry ; Antibodies, Catalytic - genetics ; Antibodies, Catalytic - metabolism ; Antibodies, Monoclonal - chemistry ; Antibodies, Monoclonal - genetics ; Antibodies, Monoclonal - metabolism ; Autoantibodies ; Base Sequence ; Binding Sites ; Biochemistry ; Catalysis ; Catalytic activity ; Chains ; Coordination compounds ; Deoxyribonucleic acid ; DNA ; DNA - chemistry ; DNA - immunology ; DNA - metabolism ; Enzymes ; Hydrolysis ; Immunoglobulin G ; In Vitro Techniques ; Kinetics ; Magnesium ; Mice ; Models, Molecular ; Mutation ; Nucleotide sequence ; Protein Conformation ; Proteins ; Studies</subject><ispartof>Applied biochemistry and biotechnology, 2000-01, Vol.83 (1-3), p.95-105</ispartof><rights>Humana Press Inc. 2000</rights><rights>Humana Press Inc. 2000.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c409t-2d887f76dae2284591b48907d34949db14b9a3cad5902171df51a5e93a2d4613</citedby></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/10826952$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rodkey, L S</creatorcontrib><creatorcontrib>Gololobov, G</creatorcontrib><creatorcontrib>Rumbley, C A</creatorcontrib><creatorcontrib>Rumbley, J</creatorcontrib><creatorcontrib>Schourov, D V</creatorcontrib><creatorcontrib>Makarevich, O I</creatorcontrib><creatorcontrib>Gabibov, A G</creatorcontrib><creatorcontrib>Voss, Jr, E W</creatorcontrib><title>DNA hydrolysis by monoclonal autoantibody BV 04-01</title><title>Applied biochemistry and biotechnology</title><addtitle>Appl Biochem Biotechnol</addtitle><description>Monoclonal anti-DNA autoantibody BV 04-01 catalyzed hydrolysis of DNA in the presence of Mg2+. Catalysis was associated with BV 04-01 IgG, Fab, and single-chain-antibody (SCA) proteins. Cleavage of both ss and dsDNA was observed with efficient hydrolysis of the C-rich region of A7C7ATATAGCGCGT2, as well as a preference for cleaving within CG-rich regions of dsDNA. Data on specificity of ssDNA hydrolysis and kinetic data obtained from wild-type SCA, and two SCA mutants were used to model the catalytically active antibody site using the previously resolved X-ray structure of BV 04-01. The resulting model suggested that the target phosphodiester bond is activated by induction of conformational strain. In addition, the antibody-DNA complex contained a Mg2+ coordination site composed of the L32Tyr and L27dHis side chains and a DNA 3'-phosphodiester group. Induction of strain along with the metal coordination could be part of the mechanism by which this antibody catalyzes DNA hydrolysis. Sequence data for BV 04-01 V(H) and V(L) genes suggested that the proposed catalytic-antibody active site was germline-encoded. This observation suggests that catalytic activity might represent an important-rarely examined-function for some antibody molecules.</description><subject>Animals</subject><subject>Antibodies</subject><subject>Antibodies, Antinuclear - chemistry</subject><subject>Antibodies, Antinuclear - genetics</subject><subject>Antibodies, Antinuclear - metabolism</subject><subject>Antibodies, Catalytic - chemistry</subject><subject>Antibodies, Catalytic - genetics</subject><subject>Antibodies, Catalytic - metabolism</subject><subject>Antibodies, Monoclonal - chemistry</subject><subject>Antibodies, Monoclonal - genetics</subject><subject>Antibodies, Monoclonal - metabolism</subject><subject>Autoantibodies</subject><subject>Base Sequence</subject><subject>Binding Sites</subject><subject>Biochemistry</subject><subject>Catalysis</subject><subject>Catalytic activity</subject><subject>Chains</subject><subject>Coordination compounds</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>DNA - chemistry</subject><subject>DNA - immunology</subject><subject>DNA - metabolism</subject><subject>Enzymes</subject><subject>Hydrolysis</subject><subject>Immunoglobulin G</subject><subject>In Vitro Techniques</subject><subject>Kinetics</subject><subject>Magnesium</subject><subject>Mice</subject><subject>Models, Molecular</subject><subject>Mutation</subject><subject>Nucleotide sequence</subject><subject>Protein Conformation</subject><subject>Proteins</subject><subject>Studies</subject><issn>0273-2289</issn><issn>0273-2289</issn><issn>1559-0291</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqF0TtPwzAQAGALgWgprIwoAgmmFJ_f7paWp1TBUrFaTuyKVmld4mTIvydVO1RIwHQ3fPewD6FLwEOgit_b3OYjRUeQ0pHmR6iPiaQpIUofH-Q9dBbjEmMgistT1AOsiNCc9BF5eMuSz9ZVoWzjIiZ5m6zCOhRlWNsysU0d7Lpe5MG1yfgjwSzFcI5O5raM_mIfB2j29DibvKTT9-fXSTZNC4Z1nRKnlJxL4azvVmBcQ86UxtJRppl2ObBcW1pYxzUmIMHNOVjuNbXEMQF0gO52bTdV-Gp8rM1qEQtflnbtQxONoloISqTq5O2fUgJQAhT_C0EKKZQiHbz5AZehqbofiYYIwSTmhGw3vP5Ngd4OFVp0aLhDRRVirPzcbKrFylatAWy2JzTZOBt3rzFgqNG8K7jad23ylXcHfHcz-g2poJIX</recordid><startdate>20000101</startdate><enddate>20000101</enddate><creator>Rodkey, L S</creator><creator>Gololobov, G</creator><creator>Rumbley, C A</creator><creator>Rumbley, J</creator><creator>Schourov, D V</creator><creator>Makarevich, O I</creator><creator>Gabibov, A G</creator><creator>Voss, Jr, E W</creator><general>Springer Nature B.V</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>3V.</scope><scope>7ST</scope><scope>7T7</scope><scope>7TM</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>SOI</scope><scope>7QO</scope><scope>7X8</scope></search><sort><creationdate>20000101</creationdate><title>DNA hydrolysis by monoclonal autoantibody BV 04-01</title><author>Rodkey, L S ; Gololobov, G ; Rumbley, C A ; Rumbley, J ; Schourov, D V ; Makarevich, O I ; Gabibov, A G ; Voss, Jr, E W</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c409t-2d887f76dae2284591b48907d34949db14b9a3cad5902171df51a5e93a2d4613</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Animals</topic><topic>Antibodies</topic><topic>Antibodies, Antinuclear - 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Academic</collection><jtitle>Applied biochemistry and biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rodkey, L S</au><au>Gololobov, G</au><au>Rumbley, C A</au><au>Rumbley, J</au><au>Schourov, D V</au><au>Makarevich, O I</au><au>Gabibov, A G</au><au>Voss, Jr, E W</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>DNA hydrolysis by monoclonal autoantibody BV 04-01</atitle><jtitle>Applied biochemistry and biotechnology</jtitle><addtitle>Appl Biochem Biotechnol</addtitle><date>2000-01-01</date><risdate>2000</risdate><volume>83</volume><issue>1-3</issue><spage>95</spage><epage>105</epage><pages>95-105</pages><issn>0273-2289</issn><eissn>0273-2289</eissn><eissn>1559-0291</eissn><abstract>Monoclonal anti-DNA autoantibody BV 04-01 catalyzed hydrolysis of DNA in the presence of Mg2+. Catalysis was associated with BV 04-01 IgG, Fab, and single-chain-antibody (SCA) proteins. Cleavage of both ss and dsDNA was observed with efficient hydrolysis of the C-rich region of A7C7ATATAGCGCGT2, as well as a preference for cleaving within CG-rich regions of dsDNA. Data on specificity of ssDNA hydrolysis and kinetic data obtained from wild-type SCA, and two SCA mutants were used to model the catalytically active antibody site using the previously resolved X-ray structure of BV 04-01. The resulting model suggested that the target phosphodiester bond is activated by induction of conformational strain. In addition, the antibody-DNA complex contained a Mg2+ coordination site composed of the L32Tyr and L27dHis side chains and a DNA 3'-phosphodiester group. Induction of strain along with the metal coordination could be part of the mechanism by which this antibody catalyzes DNA hydrolysis. Sequence data for BV 04-01 V(H) and V(L) genes suggested that the proposed catalytic-antibody active site was germline-encoded. This observation suggests that catalytic activity might represent an important-rarely examined-function for some antibody molecules.</abstract><cop>United States</cop><pub>Springer Nature B.V</pub><pmid>10826952</pmid><doi>10.1385/abab:83:1-3:95</doi><tpages>11</tpages></addata></record> |
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| subjects | Animals Antibodies Antibodies, Antinuclear - chemistry Antibodies, Antinuclear - genetics Antibodies, Antinuclear - metabolism Antibodies, Catalytic - chemistry Antibodies, Catalytic - genetics Antibodies, Catalytic - metabolism Antibodies, Monoclonal - chemistry Antibodies, Monoclonal - genetics Antibodies, Monoclonal - metabolism Autoantibodies Base Sequence Binding Sites Biochemistry Catalysis Catalytic activity Chains Coordination compounds Deoxyribonucleic acid DNA DNA - chemistry DNA - immunology DNA - metabolism Enzymes Hydrolysis Immunoglobulin G In Vitro Techniques Kinetics Magnesium Mice Models, Molecular Mutation Nucleotide sequence Protein Conformation Proteins Studies |
| title | DNA hydrolysis by monoclonal autoantibody BV 04-01 |
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