Biological characterization of a myotoxin phosphoplipase A2 homologue purified from the venom of the snake Bothrops moojeni

Bibliographic Details
Main Author: Queiroz,MR
Publication Date: 2011
Other Authors: Mamede,CC, Fonseca,KC, Canabrava,LCMN, França,LV, Silva,MC, Stanziola,L, Beletti,ME, Canabrava,HAN, Oliveira,F
Format: Article
Language: eng
Source: The Journal of venomous animals and toxins including tropical diseases (Online)
Download full: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992011000100007
Summary: A myotoxin phospholipase A2 homologue, BmooMtx, was isolated from the venom of Bothrops moojeni by a combination of ion-exchange chromatography on DEAE-Sephacel column and gel filtration on Sephadex G-75. SDS-PAGE showed the enzyme to be a monomer with a molecular weight of 16,500. BmooMtx induced release of creatine kinase and morphological analyses indicated that it provoked an intense myonecrosis, with visible leukocyte infiltrate and damaged muscle cells 24 hours after injection. Anti-BmooMTx antibodies partially neutralized the myotoxic activity of BmooMtx and crude B. moojeni venom, as judged by determination of plasma creatine kinase levels and histological evaluation of skeletal muscle in mice. Anti-BmooMTx antibodies were effective in reducing the plasma creatine kinase levels of crude B. alternatus and B. leucurus venoms, evidencing immunological cross-reactivity between BmooMTx and other bothropic venoms. Intraplantar (i.pl.) injection of BmooMtx (1 to 15 μg/animal) caused a dose- and time-dependent hyperalgesia and edematogenic responses. Dexamethasone (0.4 mg/kg), meloxicam (2 mg/kg) and promethazine (5 mg/kg) markedly reduced the hyperalgesia. Our data suggest that these drugs may likely serve as complementary therapies in cases of accidents with Bothrops moojeni, provided that such pharmacological treatments are administered immediately after the incident.
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spelling Biological characterization of a myotoxin phosphoplipase A2 homologue purified from the venom of the snake Bothrops moojeniBothrops moojenihyperalgesiamyotoxinedemaA myotoxin phospholipase A2 homologue, BmooMtx, was isolated from the venom of Bothrops moojeni by a combination of ion-exchange chromatography on DEAE-Sephacel column and gel filtration on Sephadex G-75. SDS-PAGE showed the enzyme to be a monomer with a molecular weight of 16,500. BmooMtx induced release of creatine kinase and morphological analyses indicated that it provoked an intense myonecrosis, with visible leukocyte infiltrate and damaged muscle cells 24 hours after injection. Anti-BmooMTx antibodies partially neutralized the myotoxic activity of BmooMtx and crude B. moojeni venom, as judged by determination of plasma creatine kinase levels and histological evaluation of skeletal muscle in mice. Anti-BmooMTx antibodies were effective in reducing the plasma creatine kinase levels of crude B. alternatus and B. leucurus venoms, evidencing immunological cross-reactivity between BmooMTx and other bothropic venoms. Intraplantar (i.pl.) injection of BmooMtx (1 to 15 μg/animal) caused a dose- and time-dependent hyperalgesia and edematogenic responses. Dexamethasone (0.4 mg/kg), meloxicam (2 mg/kg) and promethazine (5 mg/kg) markedly reduced the hyperalgesia. Our data suggest that these drugs may likely serve as complementary therapies in cases of accidents with Bothrops moojeni, provided that such pharmacological treatments are administered immediately after the incident.Centro de Estudos de Venenos e Animais Peçonhentos (CEVAP/UNESP)2011-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992011000100007Journal of Venomous Animals and Toxins including Tropical Diseases v.17 n.1 2011reponame:The Journal of venomous animals and toxins including tropical diseases (Online)instname:Universidade Estadual Paulista (UNESP)instacron:UNESP10.1590/S1678-91992011000100007info:eu-repo/semantics/openAccessQueiroz,MRMamede,CCFonseca,KCCanabrava,LCMNFrança,LVSilva,MCStanziola,LBeletti,MECanabrava,HANOliveira,Feng2011-03-01T00:00:00Zoai:scielo:S1678-91992011000100007Revistahttp://www.scielo.br/jvatitdPUBhttps://old.scielo.br/oai/scielo-oai.php||editorial@jvat.org.br1678-91991678-9180opendoar:2011-03-01T00:00The Journal of venomous animals and toxins including tropical diseases (Online) - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Biological characterization of a myotoxin phosphoplipase A2 homologue purified from the venom of the snake Bothrops moojeni
title Biological characterization of a myotoxin phosphoplipase A2 homologue purified from the venom of the snake Bothrops moojeni
spellingShingle Biological characterization of a myotoxin phosphoplipase A2 homologue purified from the venom of the snake Bothrops moojeni
Queiroz,MR
Bothrops moojeni
hyperalgesia
myotoxin
edema
title_short Biological characterization of a myotoxin phosphoplipase A2 homologue purified from the venom of the snake Bothrops moojeni
title_full Biological characterization of a myotoxin phosphoplipase A2 homologue purified from the venom of the snake Bothrops moojeni
title_fullStr Biological characterization of a myotoxin phosphoplipase A2 homologue purified from the venom of the snake Bothrops moojeni
title_full_unstemmed Biological characterization of a myotoxin phosphoplipase A2 homologue purified from the venom of the snake Bothrops moojeni
title_sort Biological characterization of a myotoxin phosphoplipase A2 homologue purified from the venom of the snake Bothrops moojeni
author Queiroz,MR
author_facet Queiroz,MR
Mamede,CC
Fonseca,KC
Canabrava,LCMN
França,LV
Silva,MC
Stanziola,L
Beletti,ME
Canabrava,HAN
Oliveira,F
author_role author
author2 Mamede,CC
Fonseca,KC
Canabrava,LCMN
França,LV
Silva,MC
Stanziola,L
Beletti,ME
Canabrava,HAN
Oliveira,F
author2_role author
author
author
author
author
author
author
author
author
dc.contributor.author.fl_str_mv Queiroz,MR
Mamede,CC
Fonseca,KC
Canabrava,LCMN
França,LV
Silva,MC
Stanziola,L
Beletti,ME
Canabrava,HAN
Oliveira,F
dc.subject.por.fl_str_mv Bothrops moojeni
hyperalgesia
myotoxin
edema
topic Bothrops moojeni
hyperalgesia
myotoxin
edema
description A myotoxin phospholipase A2 homologue, BmooMtx, was isolated from the venom of Bothrops moojeni by a combination of ion-exchange chromatography on DEAE-Sephacel column and gel filtration on Sephadex G-75. SDS-PAGE showed the enzyme to be a monomer with a molecular weight of 16,500. BmooMtx induced release of creatine kinase and morphological analyses indicated that it provoked an intense myonecrosis, with visible leukocyte infiltrate and damaged muscle cells 24 hours after injection. Anti-BmooMTx antibodies partially neutralized the myotoxic activity of BmooMtx and crude B. moojeni venom, as judged by determination of plasma creatine kinase levels and histological evaluation of skeletal muscle in mice. Anti-BmooMTx antibodies were effective in reducing the plasma creatine kinase levels of crude B. alternatus and B. leucurus venoms, evidencing immunological cross-reactivity between BmooMTx and other bothropic venoms. Intraplantar (i.pl.) injection of BmooMtx (1 to 15 μg/animal) caused a dose- and time-dependent hyperalgesia and edematogenic responses. Dexamethasone (0.4 mg/kg), meloxicam (2 mg/kg) and promethazine (5 mg/kg) markedly reduced the hyperalgesia. Our data suggest that these drugs may likely serve as complementary therapies in cases of accidents with Bothrops moojeni, provided that such pharmacological treatments are administered immediately after the incident.
publishDate 2011
dc.date.none.fl_str_mv 2011-01-01
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992011000100007
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992011000100007
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S1678-91992011000100007
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv text/html
dc.publisher.none.fl_str_mv Centro de Estudos de Venenos e Animais Peçonhentos (CEVAP/UNESP)
publisher.none.fl_str_mv Centro de Estudos de Venenos e Animais Peçonhentos (CEVAP/UNESP)
dc.source.none.fl_str_mv Journal of Venomous Animals and Toxins including Tropical Diseases v.17 n.1 2011
reponame:The Journal of venomous animals and toxins including tropical diseases (Online)
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str The Journal of venomous animals and toxins including tropical diseases (Online)
collection The Journal of venomous animals and toxins including tropical diseases (Online)
repository.name.fl_str_mv The Journal of venomous animals and toxins including tropical diseases (Online) - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv ||editorial@jvat.org.br
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