Conformation-dependent single-chain variable fragment antibodies specifically recognize beta-amyloid oligomers
Increasing evidence indicates that beta-amyloid (Aβ) oligomers rather than monomers or fibrils are the major toxic agents that specifically inhibit synaptic plasticity and long-term potentiation (LTP) in Alzheimer’s disease (AD). Neutralization of Aβ oligomeric toxicity was found to reverse memory d...
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| Veröffentlicht in: | FEBS letters 2009-02, Vol.583 (3), p.579-584 |
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| container_title | FEBS letters |
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| creator | Wang, Xiao-ping Zhang, Jun-hua Wang, Yu-jiong Feng, Ying Zhang, Xi Sun, Xiao-xia Li, Ji-liang Du, Xue-ting Lambert, Mary P. Yang, Shi-gao Zhao, Min Klein, William L. Liu, Rui-tian |
| description | Increasing evidence indicates that beta-amyloid (Aβ) oligomers rather than monomers or fibrils are the major toxic agents that specifically inhibit synaptic plasticity and long-term potentiation (LTP) in Alzheimer’s disease (AD). Neutralization of Aβ oligomeric toxicity was found to reverse memory deficits. Here, we report four single-chain variable fragment (scFv) antibodies isolated from the naive human scFv library by phage display that specifically recognized Aβ oligomers but not monomers and fibrils. These conformation-dependent scFv antibodies inhibit both Aβ fibrillation and cytotoxicity and bind to the same type of eptitope displayed on the Aβ oligomers. Such scFv antibodies specifically targeting toxic Aβ oligomers may have potential therapeutic and diagnostic applications for AD. |
| doi_str_mv | 10.1016/j.febslet.2008.12.064 |
| format | Article |
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Neutralization of Aβ oligomeric toxicity was found to reverse memory deficits. Here, we report four single-chain variable fragment (scFv) antibodies isolated from the naive human scFv library by phage display that specifically recognized Aβ oligomers but not monomers and fibrils. These conformation-dependent scFv antibodies inhibit both Aβ fibrillation and cytotoxicity and bind to the same type of eptitope displayed on the Aβ oligomers. Such scFv antibodies specifically targeting toxic Aβ oligomers may have potential therapeutic and diagnostic applications for AD.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/j.febslet.2008.12.064</identifier><identifier>PMID: 19162022</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyltetrazolium bromide ; ADDL ; Alzheimer's disease ; Amyloid - immunology ; Amyloid - metabolism ; Amyloid - toxicity ; amyloid β-derived diffusible ligand ; Antibodies - immunology ; Antibody Specificity - immunology ; Beta-amyloid ; beta-amyloid peptide ; Cell Line, Tumor ; Cell Survival - drug effects ; Epitope ; Epitopes - immunology ; Humans ; Kinetics ; lactate dehydrogenase ; LDH ; MTT ; Oligomer ; Protein Binding ; Protein Multimerization ; scFv ; SDS–PAGE ; Single-chain variable fragment ; sodium dodecyl sulfate–polyacrylamide gel electrophoresis ; SPR ; surface plasmon resonance</subject><ispartof>FEBS letters, 2009-02, Vol.583 (3), p.579-584</ispartof><rights>2009 Federation of European Biochemical Societies</rights><rights>FEBS Letters 583 (2009) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5064-43ba512c289fb20be052e9082f38aa5fdd4d973a0e29c4b9c9c03edc2053f85f3</citedby><cites>FETCH-LOGICAL-c5064-43ba512c289fb20be052e9082f38aa5fdd4d973a0e29c4b9c9c03edc2053f85f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2Fj.febslet.2008.12.064$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.febslet.2008.12.064$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,1416,1432,3548,27923,27924,45573,45574,45994,46408,46832</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19162022$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wang, Xiao-ping</creatorcontrib><creatorcontrib>Zhang, Jun-hua</creatorcontrib><creatorcontrib>Wang, Yu-jiong</creatorcontrib><creatorcontrib>Feng, Ying</creatorcontrib><creatorcontrib>Zhang, Xi</creatorcontrib><creatorcontrib>Sun, Xiao-xia</creatorcontrib><creatorcontrib>Li, Ji-liang</creatorcontrib><creatorcontrib>Du, Xue-ting</creatorcontrib><creatorcontrib>Lambert, Mary P.</creatorcontrib><creatorcontrib>Yang, Shi-gao</creatorcontrib><creatorcontrib>Zhao, Min</creatorcontrib><creatorcontrib>Klein, William L.</creatorcontrib><creatorcontrib>Liu, Rui-tian</creatorcontrib><title>Conformation-dependent single-chain variable fragment antibodies specifically recognize beta-amyloid oligomers</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Increasing evidence indicates that beta-amyloid (Aβ) oligomers rather than monomers or fibrils are the major toxic agents that specifically inhibit synaptic plasticity and long-term potentiation (LTP) in Alzheimer’s disease (AD). 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Such scFv antibodies specifically targeting toxic Aβ oligomers may have potential therapeutic and diagnostic applications for AD.</description><subject>3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyltetrazolium bromide</subject><subject>ADDL</subject><subject>Alzheimer's disease</subject><subject>Amyloid - immunology</subject><subject>Amyloid - metabolism</subject><subject>Amyloid - toxicity</subject><subject>amyloid β-derived diffusible ligand</subject><subject>Antibodies - immunology</subject><subject>Antibody Specificity - immunology</subject><subject>Beta-amyloid</subject><subject>beta-amyloid peptide</subject><subject>Cell Line, Tumor</subject><subject>Cell Survival - drug effects</subject><subject>Epitope</subject><subject>Epitopes - immunology</subject><subject>Humans</subject><subject>Kinetics</subject><subject>lactate dehydrogenase</subject><subject>LDH</subject><subject>MTT</subject><subject>Oligomer</subject><subject>Protein Binding</subject><subject>Protein Multimerization</subject><subject>scFv</subject><subject>SDS–PAGE</subject><subject>Single-chain variable fragment</subject><subject>sodium dodecyl sulfate–polyacrylamide gel electrophoresis</subject><subject>SPR</subject><subject>surface plasmon resonance</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkU1vEzEQhi0EomnhJ4D2xG0Xf-wm6xOCqKVIlTgAZ8sf4zCR1w72pij8erxKpB7hZI38zjszz0vIG0Y7Rtn6_b7zYEqAueOUjh3jHV33z8iKjRvRin49PicrSlnfDhsprsh1KXta65HJl-SKSbbmlPMVidsUfcqTnjHF1sEBooM4NwXjLkBrf2qMzaPOqE2Axme9m5ZvHWc0ySGUphzAokerQzg1GWzaRfwDjYFZt3o6hYSuSQF3aYJcXpEXXocCry_vDflxd_t9e98-fP38ZfvxobVDPaPthdED45aP0htODdCBg6Qj92LUevDO9U5uhKbApe2NtNJSAc5yOgg_Dl7ckHdn30NOv45QZjVhsRCCjpCORdXjh14KVoXDWWhzKiWDV4eMk84nxahaQKu9uoBWC2jFuKob1r63lwFHM4F76rqQrYL7s-A3Bjj9n6u6u_3Evy2pLaFRWQPjYpn14WwFldgjQlbFIkQLDivvWbmE_9j2L4hVqhU</recordid><startdate>20090204</startdate><enddate>20090204</enddate><creator>Wang, Xiao-ping</creator><creator>Zhang, Jun-hua</creator><creator>Wang, Yu-jiong</creator><creator>Feng, Ying</creator><creator>Zhang, Xi</creator><creator>Sun, Xiao-xia</creator><creator>Li, Ji-liang</creator><creator>Du, Xue-ting</creator><creator>Lambert, Mary P.</creator><creator>Yang, Shi-gao</creator><creator>Zhao, Min</creator><creator>Klein, William L.</creator><creator>Liu, Rui-tian</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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>7TK</scope></search><sort><creationdate>20090204</creationdate><title>Conformation-dependent single-chain variable fragment antibodies specifically recognize beta-amyloid oligomers</title><author>Wang, Xiao-ping ; Zhang, Jun-hua ; Wang, Yu-jiong ; Feng, Ying ; Zhang, Xi ; Sun, Xiao-xia ; Li, Ji-liang ; Du, Xue-ting ; Lambert, Mary P. ; Yang, Shi-gao ; Zhao, Min ; Klein, William L. ; Liu, Rui-tian</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5064-43ba512c289fb20be052e9082f38aa5fdd4d973a0e29c4b9c9c03edc2053f85f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyltetrazolium bromide</topic><topic>ADDL</topic><topic>Alzheimer's disease</topic><topic>Amyloid - immunology</topic><topic>Amyloid - metabolism</topic><topic>Amyloid - toxicity</topic><topic>amyloid β-derived diffusible ligand</topic><topic>Antibodies - immunology</topic><topic>Antibody Specificity - immunology</topic><topic>Beta-amyloid</topic><topic>beta-amyloid peptide</topic><topic>Cell Line, Tumor</topic><topic>Cell Survival - drug effects</topic><topic>Epitope</topic><topic>Epitopes - immunology</topic><topic>Humans</topic><topic>Kinetics</topic><topic>lactate dehydrogenase</topic><topic>LDH</topic><topic>MTT</topic><topic>Oligomer</topic><topic>Protein Binding</topic><topic>Protein Multimerization</topic><topic>scFv</topic><topic>SDS–PAGE</topic><topic>Single-chain variable fragment</topic><topic>sodium dodecyl sulfate–polyacrylamide gel electrophoresis</topic><topic>SPR</topic><topic>surface plasmon resonance</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wang, Xiao-ping</creatorcontrib><creatorcontrib>Zhang, Jun-hua</creatorcontrib><creatorcontrib>Wang, Yu-jiong</creatorcontrib><creatorcontrib>Feng, Ying</creatorcontrib><creatorcontrib>Zhang, Xi</creatorcontrib><creatorcontrib>Sun, Xiao-xia</creatorcontrib><creatorcontrib>Li, Ji-liang</creatorcontrib><creatorcontrib>Du, Xue-ting</creatorcontrib><creatorcontrib>Lambert, Mary P.</creatorcontrib><creatorcontrib>Yang, Shi-gao</creatorcontrib><creatorcontrib>Zhao, Min</creatorcontrib><creatorcontrib>Klein, William L.</creatorcontrib><creatorcontrib>Liu, Rui-tian</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Neurosciences Abstracts</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wang, Xiao-ping</au><au>Zhang, Jun-hua</au><au>Wang, Yu-jiong</au><au>Feng, Ying</au><au>Zhang, Xi</au><au>Sun, Xiao-xia</au><au>Li, Ji-liang</au><au>Du, Xue-ting</au><au>Lambert, Mary P.</au><au>Yang, Shi-gao</au><au>Zhao, Min</au><au>Klein, William L.</au><au>Liu, Rui-tian</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Conformation-dependent single-chain variable fragment antibodies specifically recognize beta-amyloid oligomers</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2009-02-04</date><risdate>2009</risdate><volume>583</volume><issue>3</issue><spage>579</spage><epage>584</epage><pages>579-584</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Increasing evidence indicates that beta-amyloid (Aβ) oligomers rather than monomers or fibrils are the major toxic agents that specifically inhibit synaptic plasticity and long-term potentiation (LTP) in Alzheimer’s disease (AD). Neutralization of Aβ oligomeric toxicity was found to reverse memory deficits. Here, we report four single-chain variable fragment (scFv) antibodies isolated from the naive human scFv library by phage display that specifically recognized Aβ oligomers but not monomers and fibrils. These conformation-dependent scFv antibodies inhibit both Aβ fibrillation and cytotoxicity and bind to the same type of eptitope displayed on the Aβ oligomers. Such scFv antibodies specifically targeting toxic Aβ oligomers may have potential therapeutic and diagnostic applications for AD.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>19162022</pmid><doi>10.1016/j.febslet.2008.12.064</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Wiley Free Content; ScienceDirect Journals (5 years ago - present); Wiley Online Library All Journals; Alma/SFX Local Collection |
| subjects | 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyltetrazolium bromide ADDL Alzheimer's disease Amyloid - immunology Amyloid - metabolism Amyloid - toxicity amyloid β-derived diffusible ligand Antibodies - immunology Antibody Specificity - immunology Beta-amyloid beta-amyloid peptide Cell Line, Tumor Cell Survival - drug effects Epitope Epitopes - immunology Humans Kinetics lactate dehydrogenase LDH MTT Oligomer Protein Binding Protein Multimerization scFv SDS–PAGE Single-chain variable fragment sodium dodecyl sulfate–polyacrylamide gel electrophoresis SPR surface plasmon resonance |
| title | Conformation-dependent single-chain variable fragment antibodies specifically recognize beta-amyloid oligomers |
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