Polyclonal antibodies against native weak toxin Naja kaouthia discriminate native weak toxins and some other three-fingered toxins against their denaturated forms
Polyclonal antibodies obtained by immunization of rabbits with native form of weak toxin (WTX) from cobra Naja kaouthia venom efficiently interacted with WTX and a weak toxin from Naja oxiana venom, but not so with their denaturated forms. These antibodies could also bind with lower affinity other g...
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| Veröffentlicht in: | Toxicon (Oxford) 2005-07, Vol.46 (1), p.24-30 |
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| creator | Kryukova, E.V. Mordvintsev, D.Yu Daya, S. Utkin, Yu.N. Tsetlin, V.I. |
| description | Polyclonal antibodies obtained by immunization of rabbits with native form of weak toxin (WTX) from cobra
Naja kaouthia venom efficiently interacted with WTX and a weak toxin from
Naja oxiana venom, but not so with their denaturated forms. These antibodies could also bind with lower affinity other groups of three-fingered toxins: long-chain α-neurotoxins, muscarinic toxins and cytotoxins, but practically did not bind short-chain α-neurotoxins. The efficiency of toxin–antibody interaction depends on the group (weak toxins, long or short α-neurotoxins, cytotoxins etc.) to which the toxin belongs, but not on species of snake from which the toxin originates. There is a correlation between the results obtained and phylogenetic analysis of the three-fingered toxins which revealed that WTX is very close to other weak toxins, relatively close to long α-neurotoxins, cytotoxins and muscarinic toxins, but is distant from the short α-neurotoxins. |
| doi_str_mv | 10.1016/j.toxicon.2005.03.017 |
| format | Article |
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Naja kaouthia venom efficiently interacted with WTX and a weak toxin from
Naja oxiana venom, but not so with their denaturated forms. These antibodies could also bind with lower affinity other groups of three-fingered toxins: long-chain α-neurotoxins, muscarinic toxins and cytotoxins, but practically did not bind short-chain α-neurotoxins. The efficiency of toxin–antibody interaction depends on the group (weak toxins, long or short α-neurotoxins, cytotoxins etc.) to which the toxin belongs, but not on species of snake from which the toxin originates. There is a correlation between the results obtained and phylogenetic analysis of the three-fingered toxins which revealed that WTX is very close to other weak toxins, relatively close to long α-neurotoxins, cytotoxins and muscarinic toxins, but is distant from the short α-neurotoxins.</description><identifier>ISSN: 0041-0101</identifier><identifier>EISSN: 1879-3150</identifier><identifier>DOI: 10.1016/j.toxicon.2005.03.017</identifier><identifier>PMID: 15925395</identifier><identifier>CODEN: TOXIA6</identifier><language>eng</language><publisher>Oxford: Elsevier Ltd</publisher><subject>Amino Acid Sequence ; Animals ; Antibody Affinity ; Cobra Naja kaouthia ; Elapid Venoms - chemistry ; Elapid Venoms - genetics ; Elapid Venoms - immunology ; Elapidae - physiology ; ELISA ; Epitopes ; Molecular Sequence Data ; Naja kaouthia ; Naja oxiana ; Phylogeny ; Polyclonal antibodies ; Protein Conformation ; Protein Denaturation ; Rabbits ; Three-fingered toxins ; Weak toxin</subject><ispartof>Toxicon (Oxford), 2005-07, Vol.46 (1), p.24-30</ispartof><rights>2005 Elsevier Ltd</rights><rights>2005 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c424t-7be15edd27495f811dc2b42ea2da125579f550ac5e22ac6e03c3c94b18fe20963</citedby><cites>FETCH-LOGICAL-c424t-7be15edd27495f811dc2b42ea2da125579f550ac5e22ac6e03c3c94b18fe20963</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.toxicon.2005.03.017$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>315,781,785,3551,27929,27930,46000</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=16916293$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15925395$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kryukova, E.V.</creatorcontrib><creatorcontrib>Mordvintsev, D.Yu</creatorcontrib><creatorcontrib>Daya, S.</creatorcontrib><creatorcontrib>Utkin, Yu.N.</creatorcontrib><creatorcontrib>Tsetlin, V.I.</creatorcontrib><title>Polyclonal antibodies against native weak toxin Naja kaouthia discriminate native weak toxins and some other three-fingered toxins against their denaturated forms</title><title>Toxicon (Oxford)</title><addtitle>Toxicon</addtitle><description>Polyclonal antibodies obtained by immunization of rabbits with native form of weak toxin (WTX) from cobra
Naja kaouthia venom efficiently interacted with WTX and a weak toxin from
Naja oxiana venom, but not so with their denaturated forms. These antibodies could also bind with lower affinity other groups of three-fingered toxins: long-chain α-neurotoxins, muscarinic toxins and cytotoxins, but practically did not bind short-chain α-neurotoxins. The efficiency of toxin–antibody interaction depends on the group (weak toxins, long or short α-neurotoxins, cytotoxins etc.) to which the toxin belongs, but not on species of snake from which the toxin originates. There is a correlation between the results obtained and phylogenetic analysis of the three-fingered toxins which revealed that WTX is very close to other weak toxins, relatively close to long α-neurotoxins, cytotoxins and muscarinic toxins, but is distant from the short α-neurotoxins.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antibody Affinity</subject><subject>Cobra Naja kaouthia</subject><subject>Elapid Venoms - chemistry</subject><subject>Elapid Venoms - genetics</subject><subject>Elapid Venoms - immunology</subject><subject>Elapidae - physiology</subject><subject>ELISA</subject><subject>Epitopes</subject><subject>Molecular Sequence Data</subject><subject>Naja kaouthia</subject><subject>Naja oxiana</subject><subject>Phylogeny</subject><subject>Polyclonal antibodies</subject><subject>Protein Conformation</subject><subject>Protein Denaturation</subject><subject>Rabbits</subject><subject>Three-fingered toxins</subject><subject>Weak toxin</subject><issn>0041-0101</issn><issn>1879-3150</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0ctu1DAUBmALgehQeASQN7BL8CVOxiuEKm5SBSxgbZ3YJx1PM3axnUJfhyfFo4noggUrbz7_xz4_Ic85aznj_et9W-Ivb2NoBWOqZbJlfHhANnw76EZyxR6SDWMdb1jlZ-RJznvGmNzq_jE540oLJbXakN9f43xn5xhgphCKH6PzmClcgQ-50ADF3yL9iXBNj_MC_Qx7oNcQl7LzQJ3PNvmDrw7_xTUnOJrjAWksO0y07BJiM_lwhQndX7QOq8Qn6rDmLKkGOjrFdMhPyaMJ5ozP1vOcfH__7tvFx-byy4dPF28vG9uJrjTDiFyhc2LotJq2nDsrxk4gCAdcKDXoSSkGVqEQYHtk0kqru5FvJxRM9_KcvDrl3qT4Y8FczKH-DucZAsYlGz4oJYeOV6hO0KaYc8LJ3NQdQLoznJljOWZv1nLMsRzDpKnl1Hsv1gHLeEB3f2tto4KXK4BsYZ4SBOvzves174WW1b05OazruPWYTLYeg0XnE9piXPT_ecofTUK1HQ</recordid><startdate>20050701</startdate><enddate>20050701</enddate><creator>Kryukova, E.V.</creator><creator>Mordvintsev, D.Yu</creator><creator>Daya, S.</creator><creator>Utkin, Yu.N.</creator><creator>Tsetlin, V.I.</creator><general>Elsevier Ltd</general><general>Elsevier Science</general><scope>IQODW</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>7U7</scope><scope>C1K</scope></search><sort><creationdate>20050701</creationdate><title>Polyclonal antibodies against native weak toxin Naja kaouthia discriminate native weak toxins and some other three-fingered toxins against their denaturated forms</title><author>Kryukova, E.V. ; Mordvintsev, D.Yu ; Daya, S. ; Utkin, Yu.N. ; Tsetlin, V.I.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c424t-7be15edd27495f811dc2b42ea2da125579f550ac5e22ac6e03c3c94b18fe20963</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antibody Affinity</topic><topic>Cobra Naja kaouthia</topic><topic>Elapid Venoms - chemistry</topic><topic>Elapid Venoms - genetics</topic><topic>Elapid Venoms - immunology</topic><topic>Elapidae - physiology</topic><topic>ELISA</topic><topic>Epitopes</topic><topic>Molecular Sequence Data</topic><topic>Naja kaouthia</topic><topic>Naja oxiana</topic><topic>Phylogeny</topic><topic>Polyclonal antibodies</topic><topic>Protein Conformation</topic><topic>Protein Denaturation</topic><topic>Rabbits</topic><topic>Three-fingered toxins</topic><topic>Weak toxin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kryukova, E.V.</creatorcontrib><creatorcontrib>Mordvintsev, D.Yu</creatorcontrib><creatorcontrib>Daya, S.</creatorcontrib><creatorcontrib>Utkin, Yu.N.</creatorcontrib><creatorcontrib>Tsetlin, V.I.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Toxicology Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><jtitle>Toxicon (Oxford)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kryukova, E.V.</au><au>Mordvintsev, D.Yu</au><au>Daya, S.</au><au>Utkin, Yu.N.</au><au>Tsetlin, V.I.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Polyclonal antibodies against native weak toxin Naja kaouthia discriminate native weak toxins and some other three-fingered toxins against their denaturated forms</atitle><jtitle>Toxicon (Oxford)</jtitle><addtitle>Toxicon</addtitle><date>2005-07-01</date><risdate>2005</risdate><volume>46</volume><issue>1</issue><spage>24</spage><epage>30</epage><pages>24-30</pages><issn>0041-0101</issn><eissn>1879-3150</eissn><coden>TOXIA6</coden><abstract>Polyclonal antibodies obtained by immunization of rabbits with native form of weak toxin (WTX) from cobra
Naja kaouthia venom efficiently interacted with WTX and a weak toxin from
Naja oxiana venom, but not so with their denaturated forms. These antibodies could also bind with lower affinity other groups of three-fingered toxins: long-chain α-neurotoxins, muscarinic toxins and cytotoxins, but practically did not bind short-chain α-neurotoxins. The efficiency of toxin–antibody interaction depends on the group (weak toxins, long or short α-neurotoxins, cytotoxins etc.) to which the toxin belongs, but not on species of snake from which the toxin originates. There is a correlation between the results obtained and phylogenetic analysis of the three-fingered toxins which revealed that WTX is very close to other weak toxins, relatively close to long α-neurotoxins, cytotoxins and muscarinic toxins, but is distant from the short α-neurotoxins.</abstract><cop>Oxford</cop><pub>Elsevier Ltd</pub><pmid>15925395</pmid><doi>10.1016/j.toxicon.2005.03.017</doi><tpages>7</tpages></addata></record> |
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| ispartof | Toxicon (Oxford), 2005-07, Vol.46 (1), p.24-30 |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Amino Acid Sequence Animals Antibody Affinity Cobra Naja kaouthia Elapid Venoms - chemistry Elapid Venoms - genetics Elapid Venoms - immunology Elapidae - physiology ELISA Epitopes Molecular Sequence Data Naja kaouthia Naja oxiana Phylogeny Polyclonal antibodies Protein Conformation Protein Denaturation Rabbits Three-fingered toxins Weak toxin |
| title | Polyclonal antibodies against native weak toxin Naja kaouthia discriminate native weak toxins and some other three-fingered toxins against their denaturated forms |
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