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

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 r...

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Published in:Journal of Venomous Animals and Toxins including Tropical Diseases
Main Authors: MR Queiroz, CC Mamede, KC Fonseca, LCMN Canabrava, LV França, MC Silva, L Stanziola, ME Beletti, HAN Canabrava, F Oliveira
Format: Article in Journal/Newspaper
Language:English
Published: SciELO 2011
Subjects:
Online Access:https://doi.org/10.1590/S1678-91992011000100007
https://doaj.org/article/d1800bec35064e70be6706684271b821
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spelling ftdoajarticles:oai:doaj.org/article:d1800bec35064e70be6706684271b821 2023-05-15T15:08:57+02:00 Biological characterization of a myotoxin phosphoplipase A2 homologue purified from the venom of the snake Bothrops moojeni MR Queiroz CC Mamede KC Fonseca LCMN Canabrava LV França MC Silva L Stanziola ME Beletti HAN Canabrava F Oliveira 2011-01-01T00:00:00Z https://doi.org/10.1590/S1678-91992011000100007 https://doaj.org/article/d1800bec35064e70be6706684271b821 EN eng SciELO http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992011000100007 https://doaj.org/toc/1678-9199 doi:10.1590/S1678-91992011000100007 1678-9199 https://doaj.org/article/d1800bec35064e70be6706684271b821 Journal of Venomous Animals and Toxins including Tropical Diseases, Vol 17, Iss 1, Pp 49-58 (2011) Bothrops moojeni hyperalgesia myotoxin edema Arctic medicine. Tropical medicine RC955-962 Toxicology. Poisons RA1190-1270 Zoology QL1-991 article 2011 ftdoajarticles https://doi.org/10.1590/S1678-91992011000100007 2022-12-31T00:20:03Z 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. Article in Journal/Newspaper Arctic Directory of Open Access Journals: DOAJ Articles Arctic Journal of Venomous Animals and Toxins including Tropical Diseases 17 1 49 58
institution Open Polar
collection Directory of Open Access Journals: DOAJ Articles
op_collection_id ftdoajarticles
language English
topic Bothrops moojeni
hyperalgesia
myotoxin
edema
Arctic medicine. Tropical medicine
RC955-962
Toxicology. Poisons
RA1190-1270
Zoology
QL1-991
spellingShingle Bothrops moojeni
hyperalgesia
myotoxin
edema
Arctic medicine. Tropical medicine
RC955-962
Toxicology. Poisons
RA1190-1270
Zoology
QL1-991
MR Queiroz
CC Mamede
KC Fonseca
LCMN Canabrava
LV França
MC Silva
L Stanziola
ME Beletti
HAN Canabrava
F Oliveira
Biological characterization of a myotoxin phosphoplipase A2 homologue purified from the venom of the snake Bothrops moojeni
topic_facet Bothrops moojeni
hyperalgesia
myotoxin
edema
Arctic medicine. Tropical medicine
RC955-962
Toxicology. Poisons
RA1190-1270
Zoology
QL1-991
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.
format Article in Journal/Newspaper
author MR Queiroz
CC Mamede
KC Fonseca
LCMN Canabrava
LV França
MC Silva
L Stanziola
ME Beletti
HAN Canabrava
F Oliveira
author_facet MR Queiroz
CC Mamede
KC Fonseca
LCMN Canabrava
LV França
MC Silva
L Stanziola
ME Beletti
HAN Canabrava
F Oliveira
author_sort MR Queiroz
title Biological characterization of a myotoxin phosphoplipase A2 homologue purified from the venom of the snake Bothrops moojeni
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
publisher SciELO
publishDate 2011
url https://doi.org/10.1590/S1678-91992011000100007
https://doaj.org/article/d1800bec35064e70be6706684271b821
geographic Arctic
geographic_facet Arctic
genre Arctic
genre_facet Arctic
op_source Journal of Venomous Animals and Toxins including Tropical Diseases, Vol 17, Iss 1, Pp 49-58 (2011)
op_relation http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992011000100007
https://doaj.org/toc/1678-9199
doi:10.1590/S1678-91992011000100007
1678-9199
https://doaj.org/article/d1800bec35064e70be6706684271b821
op_doi https://doi.org/10.1590/S1678-91992011000100007
container_title Journal of Venomous Animals and Toxins including Tropical Diseases
container_volume 17
container_issue 1
container_start_page 49
op_container_end_page 58
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