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A novel pentameric phospholipase A 2 myotoxin (PophPLA 2 ) from the venom of the pit viper Porthidium ophryomegas
The first toxin isolated from the venomous pit viper Porthidium ophryomegas is a basic pentameric phospholipase A (PophPLA ). Elucidation of its amino acid sequence showed that it belongs to the group IIA of secreted PLA s, with the presence of all 14 conserved cysteine positions. The toxin displaye...
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| Published in: | International journal of biological macromolecules 2018-10, Vol.118 (Pt A), p.1 |
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| Main Authors: | , , , , , , |
| Format: | Article |
| Language: | English |
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| container_issue | Pt A |
| container_start_page | 1 |
| container_title | International journal of biological macromolecules |
| container_volume | 118 |
| creator | Vindas, Julio Carrera, Yarina Lomonte, Bruno Gutiérrez, José María Calvete, Juan J Sanz, Libia Fernández, Julián |
| description | The first toxin isolated from the venomous pit viper Porthidium ophryomegas is a basic pentameric phospholipase A
(PophPLA
). Elucidation of its amino acid sequence showed that it belongs to the group IIA of secreted PLA
s, with the presence of all 14 conserved cysteine positions. The toxin displayed catalytic activity, in agreement with the presence of Asp49 in its sequence of 121 residues. SDS-PAGE analysis revealed that this toxin is pentameric in non-reducing conditions, a structural organization that has not been described for any viperid PLA
. PophPLA
displayed moderate myotoxic (in vivo) and cytotoxic (in vitro) activities, as well as anticoagulant activity on human plasma (in vitro). PophPLA
was not lethal, and did not induce signs of toxicity or distress in mice, when administered intravenously at a dose of up to 100 μg (5.9 μg/g). The toxin showed highest sequence identity with other PLA
s from the venoms of ancestral Asian pit viper species. |
| doi_str_mv | 10.1016/j.ijbiomac.2018.06.028 |
| format | article |
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(PophPLA
). Elucidation of its amino acid sequence showed that it belongs to the group IIA of secreted PLA
s, with the presence of all 14 conserved cysteine positions. The toxin displayed catalytic activity, in agreement with the presence of Asp49 in its sequence of 121 residues. SDS-PAGE analysis revealed that this toxin is pentameric in non-reducing conditions, a structural organization that has not been described for any viperid PLA
. PophPLA
displayed moderate myotoxic (in vivo) and cytotoxic (in vitro) activities, as well as anticoagulant activity on human plasma (in vitro). PophPLA
was not lethal, and did not induce signs of toxicity or distress in mice, when administered intravenously at a dose of up to 100 μg (5.9 μg/g). The toxin showed highest sequence identity with other PLA
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(PophPLA
). Elucidation of its amino acid sequence showed that it belongs to the group IIA of secreted PLA
s, with the presence of all 14 conserved cysteine positions. The toxin displayed catalytic activity, in agreement with the presence of Asp49 in its sequence of 121 residues. SDS-PAGE analysis revealed that this toxin is pentameric in non-reducing conditions, a structural organization that has not been described for any viperid PLA
. PophPLA
displayed moderate myotoxic (in vivo) and cytotoxic (in vitro) activities, as well as anticoagulant activity on human plasma (in vitro). PophPLA
was not lethal, and did not induce signs of toxicity or distress in mice, when administered intravenously at a dose of up to 100 μg (5.9 μg/g). The toxin showed highest sequence identity with other PLA
s from the venoms of ancestral Asian pit viper species.</description><subject>Amino Acid Sequence - genetics</subject><subject>Animals</subject><subject>Crotalid Venoms - chemistry</subject><subject>Crotalid Venoms - enzymology</subject><subject>Crotalid Venoms - genetics</subject><subject>Crotalid Venoms - pharmacology</subject><subject>Crotalinae</subject><subject>Humans</subject><subject>Mice</subject><subject>Phospholipases A2 - chemistry</subject><subject>Phospholipases A2 - genetics</subject><subject>Phospholipases A2 - pharmacology</subject><issn>1879-0003</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><recordid>eNqFTj1PwzAQtZAQLdC_UN0IQ107VVN3rBCIgSFD98ptL_iiOGdsNyL_noBgZnh6n8MTYq6V1EqXy0ZScyT29iQLpY1UpVSFuRJTbTbbhVJqNRG3KTWjKtfa3IhJsTWm1Bs9FR876LjHFgJ22XqMdILgOI1oKdiEsIMC_MCZP6mDh4qDq96-s0eoI3vIDqHHblRc_5hAGXoKGKHimB2d6TJ2wcWBPb7bdC-ua9smnP3ynZi_PO-fXhfhcvR4PoRI3sbh8Pdx9e_gCxDJT0E</recordid><startdate>20181015</startdate><enddate>20181015</enddate><creator>Vindas, Julio</creator><creator>Carrera, Yarina</creator><creator>Lomonte, Bruno</creator><creator>Gutiérrez, José María</creator><creator>Calvete, Juan J</creator><creator>Sanz, Libia</creator><creator>Fernández, Julián</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope></search><sort><creationdate>20181015</creationdate><title>A novel pentameric phospholipase A 2 myotoxin (PophPLA 2 ) from the venom of the pit viper Porthidium ophryomegas</title><author>Vindas, Julio ; Carrera, Yarina ; Lomonte, Bruno ; Gutiérrez, José María ; Calvete, Juan J ; Sanz, Libia ; Fernández, Julián</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-pubmed_primary_298861713</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Amino Acid Sequence - genetics</topic><topic>Animals</topic><topic>Crotalid Venoms - chemistry</topic><topic>Crotalid Venoms - enzymology</topic><topic>Crotalid Venoms - genetics</topic><topic>Crotalid Venoms - pharmacology</topic><topic>Crotalinae</topic><topic>Humans</topic><topic>Mice</topic><topic>Phospholipases A2 - chemistry</topic><topic>Phospholipases A2 - genetics</topic><topic>Phospholipases A2 - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Vindas, Julio</creatorcontrib><creatorcontrib>Carrera, Yarina</creatorcontrib><creatorcontrib>Lomonte, Bruno</creatorcontrib><creatorcontrib>Gutiérrez, José María</creatorcontrib><creatorcontrib>Calvete, Juan J</creatorcontrib><creatorcontrib>Sanz, Libia</creatorcontrib><creatorcontrib>Fernández, Julián</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><jtitle>International journal of biological macromolecules</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Vindas, Julio</au><au>Carrera, Yarina</au><au>Lomonte, Bruno</au><au>Gutiérrez, José María</au><au>Calvete, Juan J</au><au>Sanz, Libia</au><au>Fernández, Julián</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A novel pentameric phospholipase A 2 myotoxin (PophPLA 2 ) from the venom of the pit viper Porthidium ophryomegas</atitle><jtitle>International journal of biological macromolecules</jtitle><addtitle>Int J Biol Macromol</addtitle><date>2018-10-15</date><risdate>2018</risdate><volume>118</volume><issue>Pt A</issue><spage>1</spage><pages>1-</pages><eissn>1879-0003</eissn><abstract>The first toxin isolated from the venomous pit viper Porthidium ophryomegas is a basic pentameric phospholipase A
(PophPLA
). Elucidation of its amino acid sequence showed that it belongs to the group IIA of secreted PLA
s, with the presence of all 14 conserved cysteine positions. The toxin displayed catalytic activity, in agreement with the presence of Asp49 in its sequence of 121 residues. SDS-PAGE analysis revealed that this toxin is pentameric in non-reducing conditions, a structural organization that has not been described for any viperid PLA
. PophPLA
displayed moderate myotoxic (in vivo) and cytotoxic (in vitro) activities, as well as anticoagulant activity on human plasma (in vitro). PophPLA
was not lethal, and did not induce signs of toxicity or distress in mice, when administered intravenously at a dose of up to 100 μg (5.9 μg/g). The toxin showed highest sequence identity with other PLA
s from the venoms of ancestral Asian pit viper species.</abstract><cop>Netherlands</cop><pmid>29886171</pmid><doi>10.1016/j.ijbiomac.2018.06.028</doi></addata></record> |
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| identifier | EISSN: 1879-0003 |
| ispartof | International journal of biological macromolecules, 2018-10, Vol.118 (Pt A), p.1 |
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| source | ScienceDirect Freedom Collection |
| subjects | Amino Acid Sequence - genetics Animals Crotalid Venoms - chemistry Crotalid Venoms - enzymology Crotalid Venoms - genetics Crotalid Venoms - pharmacology Crotalinae Humans Mice Phospholipases A2 - chemistry Phospholipases A2 - genetics Phospholipases A2 - pharmacology |
| title | A novel pentameric phospholipase A 2 myotoxin (PophPLA 2 ) from the venom of the pit viper Porthidium ophryomegas |
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