Bcs T x3 is a founder of a novel sea anemone toxin family of potassium channel blocker
Sea anemone venoms have become a rich source of peptide toxins which are invaluable tools for studying the structure and functions of ion channels. In this work, BcsTx3, a toxin found in the venom of a B unodosoma caissarum (population captured at the S aint P eter and S aint P aul A rchipelago, B r...
Gespeichert in:
| Veröffentlicht in: | The FEBS journal 2013-10, Vol.280 (19), p.4839-4852 |
|---|---|
| Hauptverfasser: | , , , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 4852 |
|---|---|
| container_issue | 19 |
| container_start_page | 4839 |
| container_title | The FEBS journal |
| container_volume | 280 |
| creator | Orts, Diego J. B. Moran, Yehu Cologna, Camila T. Peigneur, Steve Madio, Bruno Praher, Daniela Quinton, Loic De Pauw, Edwin Bicudo, José E. P. W. Tytgat, Jan de Freitas, José C. |
| description | Sea anemone venoms have become a rich source of peptide toxins which are invaluable tools for studying the structure and functions of ion channels. In this work, BcsTx3, a toxin found in the venom of a
B
unodosoma caissarum
(population captured at the
S
aint
P
eter and
S
aint
P
aul
A
rchipelago,
B
razil) was purified and biochemically and pharmacologically characterized. The pharmacological effects were studied on 12 different subtypes of voltage‐gated potassium channels (K
V
1.1–K
V
1.6; K
V
2.1; K
V
3.1; K
V
4.2; K
V
4.3;
h
ERG and Shaker IR) and three cloned voltage‐gated sodium channel isoforms (Na
V
1.2, Na
V
1.4 and BgNa
V
1.1) expressed in
X
enopus laevis
oocytes. BcsTx3 shows a high affinity for
D
rosophila
S
haker
IR
channels over rKv1.2, hKv1.3 and rKv1.6, and is not active on Na
V
channels. Biochemical characterization reveals that BcsTx3 is a 50 amino acid peptide crosslinked by four disulfide bridges, and sequence comparison allowed BcsTx3 to be classified as a novel type of sea anemone toxin acting on K
V
channels. Moreover, putative toxins homologous to BcsTx3 from two additional actiniarian species suggest an ancient origin of this newly discovered toxin family. |
| doi_str_mv | 10.1111/febs.12456 |
| format | Article |
| fullrecord | <record><control><sourceid>crossref</sourceid><recordid>TN_cdi_crossref_primary_10_1111_febs_12456</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>10_1111_febs_12456</sourcerecordid><originalsourceid>FETCH-LOGICAL-c766-8a790eefb4e6338b71c41f343e1175b61690b08c74246d88ca9c51b0d0a4a2ee3</originalsourceid><addsrcrecordid>eNo9kNFKwzAUhoMoOKc3PkGuhc6kSdP0UofOwWA3RbwrJ-kJVttkJJtsb2-r4n9z_gMfh8NHyC1nCz7m3qFJC57LQp2RGS9lnklV6PP_Lt8uyVVKH4yJQlbVjLw-2kRrehS0SxSoCwffYqTBjYsPX9jThEDB4xA80n04dp46GLr-NDG7sIeUusNA7Tt4P9KmD_YT4zW5cNAnvPmbc1I_P9XLl2yzXa2XD5vMlkplGsqKITojUQmhTcmt5E5IgZyXhVFcVcwwbcffpWq1tlDZghvWMpCQI4o5ufs9a2NIKaJrdrEbIJ4azppJSDMJaX6EiG8YZ1Np</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Bcs T x3 is a founder of a novel sea anemone toxin family of potassium channel blocker</title><source>Access via Wiley Online Library</source><source>IngentaConnect Free/Open Access Journals</source><source>Wiley Online Library (Open Access Collection)</source><source>Free Full-Text Journals in Chemistry</source><creator>Orts, Diego J. B. ; Moran, Yehu ; Cologna, Camila T. ; Peigneur, Steve ; Madio, Bruno ; Praher, Daniela ; Quinton, Loic ; De Pauw, Edwin ; Bicudo, José E. P. W. ; Tytgat, Jan ; de Freitas, José C.</creator><creatorcontrib>Orts, Diego J. B. ; Moran, Yehu ; Cologna, Camila T. ; Peigneur, Steve ; Madio, Bruno ; Praher, Daniela ; Quinton, Loic ; De Pauw, Edwin ; Bicudo, José E. P. W. ; Tytgat, Jan ; de Freitas, José C.</creatorcontrib><description>Sea anemone venoms have become a rich source of peptide toxins which are invaluable tools for studying the structure and functions of ion channels. In this work, BcsTx3, a toxin found in the venom of a
B
unodosoma caissarum
(population captured at the
S
aint
P
eter and
S
aint
P
aul
A
rchipelago,
B
razil) was purified and biochemically and pharmacologically characterized. The pharmacological effects were studied on 12 different subtypes of voltage‐gated potassium channels (K
V
1.1–K
V
1.6; K
V
2.1; K
V
3.1; K
V
4.2; K
V
4.3;
h
ERG and Shaker IR) and three cloned voltage‐gated sodium channel isoforms (Na
V
1.2, Na
V
1.4 and BgNa
V
1.1) expressed in
X
enopus laevis
oocytes. BcsTx3 shows a high affinity for
D
rosophila
S
haker
IR
channels over rKv1.2, hKv1.3 and rKv1.6, and is not active on Na
V
channels. Biochemical characterization reveals that BcsTx3 is a 50 amino acid peptide crosslinked by four disulfide bridges, and sequence comparison allowed BcsTx3 to be classified as a novel type of sea anemone toxin acting on K
V
channels. Moreover, putative toxins homologous to BcsTx3 from two additional actiniarian species suggest an ancient origin of this newly discovered toxin family.</description><identifier>ISSN: 1742-464X</identifier><identifier>EISSN: 1742-4658</identifier><identifier>DOI: 10.1111/febs.12456</identifier><language>eng</language><ispartof>The FEBS journal, 2013-10, Vol.280 (19), p.4839-4852</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c766-8a790eefb4e6338b71c41f343e1175b61690b08c74246d88ca9c51b0d0a4a2ee3</citedby><cites>FETCH-LOGICAL-c766-8a790eefb4e6338b71c41f343e1175b61690b08c74246d88ca9c51b0d0a4a2ee3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,781,785,27929,27930</link.rule.ids></links><search><creatorcontrib>Orts, Diego J. B.</creatorcontrib><creatorcontrib>Moran, Yehu</creatorcontrib><creatorcontrib>Cologna, Camila T.</creatorcontrib><creatorcontrib>Peigneur, Steve</creatorcontrib><creatorcontrib>Madio, Bruno</creatorcontrib><creatorcontrib>Praher, Daniela</creatorcontrib><creatorcontrib>Quinton, Loic</creatorcontrib><creatorcontrib>De Pauw, Edwin</creatorcontrib><creatorcontrib>Bicudo, José E. P. W.</creatorcontrib><creatorcontrib>Tytgat, Jan</creatorcontrib><creatorcontrib>de Freitas, José C.</creatorcontrib><title>Bcs T x3 is a founder of a novel sea anemone toxin family of potassium channel blocker</title><title>The FEBS journal</title><description>Sea anemone venoms have become a rich source of peptide toxins which are invaluable tools for studying the structure and functions of ion channels. In this work, BcsTx3, a toxin found in the venom of a
B
unodosoma caissarum
(population captured at the
S
aint
P
eter and
S
aint
P
aul
A
rchipelago,
B
razil) was purified and biochemically and pharmacologically characterized. The pharmacological effects were studied on 12 different subtypes of voltage‐gated potassium channels (K
V
1.1–K
V
1.6; K
V
2.1; K
V
3.1; K
V
4.2; K
V
4.3;
h
ERG and Shaker IR) and three cloned voltage‐gated sodium channel isoforms (Na
V
1.2, Na
V
1.4 and BgNa
V
1.1) expressed in
X
enopus laevis
oocytes. BcsTx3 shows a high affinity for
D
rosophila
S
haker
IR
channels over rKv1.2, hKv1.3 and rKv1.6, and is not active on Na
V
channels. Biochemical characterization reveals that BcsTx3 is a 50 amino acid peptide crosslinked by four disulfide bridges, and sequence comparison allowed BcsTx3 to be classified as a novel type of sea anemone toxin acting on K
V
channels. Moreover, putative toxins homologous to BcsTx3 from two additional actiniarian species suggest an ancient origin of this newly discovered toxin family.</description><issn>1742-464X</issn><issn>1742-4658</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><recordid>eNo9kNFKwzAUhoMoOKc3PkGuhc6kSdP0UofOwWA3RbwrJ-kJVttkJJtsb2-r4n9z_gMfh8NHyC1nCz7m3qFJC57LQp2RGS9lnklV6PP_Lt8uyVVKH4yJQlbVjLw-2kRrehS0SxSoCwffYqTBjYsPX9jThEDB4xA80n04dp46GLr-NDG7sIeUusNA7Tt4P9KmD_YT4zW5cNAnvPmbc1I_P9XLl2yzXa2XD5vMlkplGsqKITojUQmhTcmt5E5IgZyXhVFcVcwwbcffpWq1tlDZghvWMpCQI4o5ufs9a2NIKaJrdrEbIJ4azppJSDMJaX6EiG8YZ1Np</recordid><startdate>201310</startdate><enddate>201310</enddate><creator>Orts, Diego J. B.</creator><creator>Moran, Yehu</creator><creator>Cologna, Camila T.</creator><creator>Peigneur, Steve</creator><creator>Madio, Bruno</creator><creator>Praher, Daniela</creator><creator>Quinton, Loic</creator><creator>De Pauw, Edwin</creator><creator>Bicudo, José E. P. W.</creator><creator>Tytgat, Jan</creator><creator>de Freitas, José C.</creator><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>201310</creationdate><title>Bcs T x3 is a founder of a novel sea anemone toxin family of potassium channel blocker</title><author>Orts, Diego J. B. ; Moran, Yehu ; Cologna, Camila T. ; Peigneur, Steve ; Madio, Bruno ; Praher, Daniela ; Quinton, Loic ; De Pauw, Edwin ; Bicudo, José E. P. W. ; Tytgat, Jan ; de Freitas, José C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c766-8a790eefb4e6338b71c41f343e1175b61690b08c74246d88ca9c51b0d0a4a2ee3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Orts, Diego J. B.</creatorcontrib><creatorcontrib>Moran, Yehu</creatorcontrib><creatorcontrib>Cologna, Camila T.</creatorcontrib><creatorcontrib>Peigneur, Steve</creatorcontrib><creatorcontrib>Madio, Bruno</creatorcontrib><creatorcontrib>Praher, Daniela</creatorcontrib><creatorcontrib>Quinton, Loic</creatorcontrib><creatorcontrib>De Pauw, Edwin</creatorcontrib><creatorcontrib>Bicudo, José E. P. W.</creatorcontrib><creatorcontrib>Tytgat, Jan</creatorcontrib><creatorcontrib>de Freitas, José C.</creatorcontrib><collection>CrossRef</collection><jtitle>The FEBS journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Orts, Diego J. B.</au><au>Moran, Yehu</au><au>Cologna, Camila T.</au><au>Peigneur, Steve</au><au>Madio, Bruno</au><au>Praher, Daniela</au><au>Quinton, Loic</au><au>De Pauw, Edwin</au><au>Bicudo, José E. P. W.</au><au>Tytgat, Jan</au><au>de Freitas, José C.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Bcs T x3 is a founder of a novel sea anemone toxin family of potassium channel blocker</atitle><jtitle>The FEBS journal</jtitle><date>2013-10</date><risdate>2013</risdate><volume>280</volume><issue>19</issue><spage>4839</spage><epage>4852</epage><pages>4839-4852</pages><issn>1742-464X</issn><eissn>1742-4658</eissn><abstract>Sea anemone venoms have become a rich source of peptide toxins which are invaluable tools for studying the structure and functions of ion channels. In this work, BcsTx3, a toxin found in the venom of a
B
unodosoma caissarum
(population captured at the
S
aint
P
eter and
S
aint
P
aul
A
rchipelago,
B
razil) was purified and biochemically and pharmacologically characterized. The pharmacological effects were studied on 12 different subtypes of voltage‐gated potassium channels (K
V
1.1–K
V
1.6; K
V
2.1; K
V
3.1; K
V
4.2; K
V
4.3;
h
ERG and Shaker IR) and three cloned voltage‐gated sodium channel isoforms (Na
V
1.2, Na
V
1.4 and BgNa
V
1.1) expressed in
X
enopus laevis
oocytes. BcsTx3 shows a high affinity for
D
rosophila
S
haker
IR
channels over rKv1.2, hKv1.3 and rKv1.6, and is not active on Na
V
channels. Biochemical characterization reveals that BcsTx3 is a 50 amino acid peptide crosslinked by four disulfide bridges, and sequence comparison allowed BcsTx3 to be classified as a novel type of sea anemone toxin acting on K
V
channels. Moreover, putative toxins homologous to BcsTx3 from two additional actiniarian species suggest an ancient origin of this newly discovered toxin family.</abstract><doi>10.1111/febs.12456</doi><tpages>14</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1742-464X |
| ispartof | The FEBS journal, 2013-10, Vol.280 (19), p.4839-4852 |
| issn | 1742-464X 1742-4658 |
| language | eng |
| recordid | cdi_crossref_primary_10_1111_febs_12456 |
| source | Access via Wiley Online Library; IngentaConnect Free/Open Access Journals; Wiley Online Library (Open Access Collection); Free Full-Text Journals in Chemistry |
| title | Bcs T x3 is a founder of a novel sea anemone toxin family of potassium channel blocker |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-11T15%3A53%3A08IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-crossref&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Bcs%20T%20x3%20is%20a%20founder%20of%20a%20novel%20sea%20anemone%20toxin%20family%20of%20potassium%20channel%20blocker&rft.jtitle=The%20FEBS%20journal&rft.au=Orts,%20Diego%20J.%20B.&rft.date=2013-10&rft.volume=280&rft.issue=19&rft.spage=4839&rft.epage=4852&rft.pages=4839-4852&rft.issn=1742-464X&rft.eissn=1742-4658&rft_id=info:doi/10.1111/febs.12456&rft_dat=%3Ccrossref%3E10_1111_febs_12456%3C/crossref%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_id=info:pmid/&rfr_iscdi=true |