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...
Published in: | Journal of Venomous Animals and Toxins including Tropical Diseases |
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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 |
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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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1766340214003859456 |