First tryptophan-containing weak neurotoxin from cobra venom
With the purpose of studying structure-function relationships among weak neurotoxins (called so because of their low toxicity), we have isolated a toxin (WTX) from the venom of cobra Naja kaouthia using a combination of gel-filtration and ion-exchange chromatography. The amino acid sequence of the i...
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| Veröffentlicht in: | Toxicon (Oxford) 2001-07, Vol.39 (7), p.921-927 |
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| container_title | Toxicon (Oxford) |
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| creator | UTKIN, Y. N KUKHTINA, V. V MASLENNIKOV, I. V ELETSKY, A. V STARKOV, V. G WEISE, C FRANKE, P HUCHO, F TSETLIN, V. I |
| description | With the purpose of studying structure-function relationships among weak neurotoxins (called so because of their low toxicity), we have isolated a toxin (WTX) from the venom of cobra Naja kaouthia using a combination of gel-filtration and ion-exchange chromatography. The amino acid sequence of the isolated toxin was determined by means of Edman degradation and MALDI mass spectrometry, the primary structure obtained being confirmed by 1H-NMR in the course of spatial structure analysis. The WTX sequence differs slightly from that of the toxin CM-9a isolated earlier from the same venom (Joubert and Taljaard, Hoppe-Seyler's Z. Physiol. Chem., 361 (1980) 425). The differences include an extra residue (Trp36) between Ser35 and Arg37 as well as interchanging of two residues (Tyr52 and Lys50) in the C-terminal part of the toxin molecule. These changes improve the alignment that can be made with other weak neurotoxin sequences. An extended sequence comparison reveals that WTX is the first case of a tryptophan-containing weak neurotoxin isolated from cobra venom. WTX was found to compete with radioiodinated alpha-bungarotoxin for binding to the membrane-bound nicotinic acetylcholine receptor from Torpedo californica. |
| doi_str_mv | 10.1016/S0041-0101(00)00223-3 |
| format | Article |
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N ; KUKHTINA, V. V ; MASLENNIKOV, I. V ; ELETSKY, A. V ; STARKOV, V. G ; WEISE, C ; FRANKE, P ; HUCHO, F ; TSETLIN, V. I</creator><creatorcontrib>UTKIN, Y. N ; KUKHTINA, V. V ; MASLENNIKOV, I. V ; ELETSKY, A. V ; STARKOV, V. G ; WEISE, C ; FRANKE, P ; HUCHO, F ; TSETLIN, V. I</creatorcontrib><description>With the purpose of studying structure-function relationships among weak neurotoxins (called so because of their low toxicity), we have isolated a toxin (WTX) from the venom of cobra Naja kaouthia using a combination of gel-filtration and ion-exchange chromatography. The amino acid sequence of the isolated toxin was determined by means of Edman degradation and MALDI mass spectrometry, the primary structure obtained being confirmed by 1H-NMR in the course of spatial structure analysis. The WTX sequence differs slightly from that of the toxin CM-9a isolated earlier from the same venom (Joubert and Taljaard, Hoppe-Seyler's Z. Physiol. Chem., 361 (1980) 425). The differences include an extra residue (Trp36) between Ser35 and Arg37 as well as interchanging of two residues (Tyr52 and Lys50) in the C-terminal part of the toxin molecule. These changes improve the alignment that can be made with other weak neurotoxin sequences. An extended sequence comparison reveals that WTX is the first case of a tryptophan-containing weak neurotoxin isolated from cobra venom. 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The amino acid sequence of the isolated toxin was determined by means of Edman degradation and MALDI mass spectrometry, the primary structure obtained being confirmed by 1H-NMR in the course of spatial structure analysis. The WTX sequence differs slightly from that of the toxin CM-9a isolated earlier from the same venom (Joubert and Taljaard, Hoppe-Seyler's Z. Physiol. Chem., 361 (1980) 425). The differences include an extra residue (Trp36) between Ser35 and Arg37 as well as interchanging of two residues (Tyr52 and Lys50) in the C-terminal part of the toxin molecule. These changes improve the alignment that can be made with other weak neurotoxin sequences. An extended sequence comparison reveals that WTX is the first case of a tryptophan-containing weak neurotoxin isolated from cobra venom. WTX was found to compete with radioiodinated alpha-bungarotoxin for binding to the membrane-bound nicotinic acetylcholine receptor from Torpedo californica.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Elapid Venoms - chemistry</subject><subject>Elapid Venoms - toxicity</subject><subject>Hydrolysis</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Naja kaouthia</subject><subject>Neurotoxins - chemistry</subject><subject>Neurotoxins - isolation & purification</subject><subject>Neurotoxins - toxicity</subject><subject>Receptors, Nicotinic - drug effects</subject><subject>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</subject><subject>Torpedo</subject><subject>Torpedo californica</subject><subject>Trypsin</subject><subject>Tryptophan - chemistry</subject><issn>0041-0101</issn><issn>1879-3150</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkMFKxDAQhoMo7rr6CEpBED1UZ5q2acCLLK4KCx7Uc0jTVKttUpNW3be3u5b1NHP4_n-Gj5BjhEsETK-eAGIMYdjPAS4AooiGdIdMMWM8pJjALplukQk58P4dAGjG030yQRxwYHxKrheV813QuVXb2fZNmlBZ08nKVOY1-NbyIzC6d7azP5UJSmebQNncyeBLG9sckr1S1l4fjXNGXha3z_P7cPl49zC_WYYqxrQLVU6LqFQ8QoaQI-YRB11wjKksKUMcfucq1WVSQqJpEWdJwWLKM6UTpookpTNy9tfbOvvZa9-JpvJK17U02vZeIMtYhjQawOQPVM5673QpWlc10q0EglhrExttYu1EAIiNNkGH3Ml4oM8bXfynRk8DcDoC0itZl04aVfktx5FFyOkvlPN0Fw</recordid><startdate>20010701</startdate><enddate>20010701</enddate><creator>UTKIN, Y. 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N</creatorcontrib><creatorcontrib>KUKHTINA, V. V</creatorcontrib><creatorcontrib>MASLENNIKOV, I. V</creatorcontrib><creatorcontrib>ELETSKY, A. V</creatorcontrib><creatorcontrib>STARKOV, V. G</creatorcontrib><creatorcontrib>WEISE, C</creatorcontrib><creatorcontrib>FRANKE, P</creatorcontrib><creatorcontrib>HUCHO, F</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>Neurosciences Abstracts</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>UTKIN, Y. N</au><au>KUKHTINA, V. V</au><au>MASLENNIKOV, I. V</au><au>ELETSKY, A. V</au><au>STARKOV, V. G</au><au>WEISE, C</au><au>FRANKE, P</au><au>HUCHO, F</au><au>TSETLIN, V. I</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>First tryptophan-containing weak neurotoxin from cobra venom</atitle><jtitle>Toxicon (Oxford)</jtitle><addtitle>Toxicon</addtitle><date>2001-07-01</date><risdate>2001</risdate><volume>39</volume><issue>7</issue><spage>921</spage><epage>927</epage><pages>921-927</pages><issn>0041-0101</issn><eissn>1879-3150</eissn><coden>TOXIA6</coden><abstract>With the purpose of studying structure-function relationships among weak neurotoxins (called so because of their low toxicity), we have isolated a toxin (WTX) from the venom of cobra Naja kaouthia using a combination of gel-filtration and ion-exchange chromatography. The amino acid sequence of the isolated toxin was determined by means of Edman degradation and MALDI mass spectrometry, the primary structure obtained being confirmed by 1H-NMR in the course of spatial structure analysis. The WTX sequence differs slightly from that of the toxin CM-9a isolated earlier from the same venom (Joubert and Taljaard, Hoppe-Seyler's Z. Physiol. Chem., 361 (1980) 425). The differences include an extra residue (Trp36) between Ser35 and Arg37 as well as interchanging of two residues (Tyr52 and Lys50) in the C-terminal part of the toxin molecule. These changes improve the alignment that can be made with other weak neurotoxin sequences. An extended sequence comparison reveals that WTX is the first case of a tryptophan-containing weak neurotoxin isolated from cobra venom. 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| subjects | Amino Acid Sequence Animals Elapid Venoms - chemistry Elapid Venoms - toxicity Hydrolysis Magnetic Resonance Spectroscopy Mice Molecular Sequence Data Naja kaouthia Neurotoxins - chemistry Neurotoxins - isolation & purification Neurotoxins - toxicity Receptors, Nicotinic - drug effects Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Torpedo Torpedo californica Trypsin Tryptophan - chemistry |
| title | First tryptophan-containing weak neurotoxin from cobra venom |
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