Molecular cloning of a hyaluronidase fromBothrops pauloensisvenom gland
Background Hyaluronate is one of the major components of extracellular matrix from vertebrates whose breakdown is catalyzed by the enzyme hyaluronidase. These enzymes are widely described in snake venoms, in which they facilitate the spreading of the main toxins in the victim’s body during the enven...
Published in: | Journal of Venomous Animals and Toxins including Tropical Diseases |
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ftdoajarticles:oai:doaj.org/article:f778258145b24e449da977a56a49f205 2023-05-15T15:15:25+02:00 Molecular cloning of a hyaluronidase fromBothrops pauloensisvenom gland Letícia Eulalio Castanheira Renata Santos Rodrigues Johara Boldrini-França Fernando PP Fonseca Flávio Henrique-Silva Maria I Homsi-Brandeburgo Veridiana M Rodrigues 2014-08-01T00:00:00Z https://doi.org/10.1186/1678-9199-20-25 https://doaj.org/article/f778258145b24e449da977a56a49f205 EN eng SciELO http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992014000200330&lng=en&tlng=en https://doaj.org/toc/1678-9199 1678-9199 doi:10.1186/1678-9199-20-25 https://doaj.org/article/f778258145b24e449da977a56a49f205 Journal of Venomous Animals and Toxins including Tropical Diseases, Vol 20, Iss 0 (2014) Alternative splicing Hyaluronidase-like Snake venom Arctic medicine. Tropical medicine RC955-962 Toxicology. Poisons RA1190-1270 Zoology QL1-991 article 2014 ftdoajarticles https://doi.org/10.1186/1678-9199-20-25 2022-12-31T02:24:44Z Background Hyaluronate is one of the major components of extracellular matrix from vertebrates whose breakdown is catalyzed by the enzyme hyaluronidase. These enzymes are widely described in snake venoms, in which they facilitate the spreading of the main toxins in the victim’s body during the envenoming. Snake venoms also present some variants (hyaluronidases-like substances) that are probably originated by alternative splicing, even though their relevance in envenomation is still under investigation. Hyaluronidases-like proteins have not yet been purified from any snake venom, but the cDNA that encodes these toxins was already identified in snake venom glands by transcriptomic analysis. Herein, we report the cloning and in silicoanalysis of the first hyaluronidase-like proteins from a Brazilian snake venom.Methods The cDNA sequence of hyaluronidase was cloned from the transcriptome of Bothrops pauloensisvenom glands. This sequence was submitted to multiple alignment with other related sequences by ClustalW. A phylogenetic analysis was performed using MEGA 4 software by the neighbor joining (NJ) method.Results The cDNA from Bothrops pauloensis venom gland that corresponds to hyaluronidase comprises 1175 bp and codifies a protein containing 194 amino acid residues. The sequence, denominated BpHyase, was identified as hyaluronidase-like since it shows high sequence identities (above 83%) with other described snake venom hyaluronidase-like sequences. Hyaluronidases-like proteins are thought to be products of alternative splicing implicated in deletions of central amino acids, including the catalytic residues. Structure-based sequence alignment of BpHyase to human hyaluronidase hHyal-1 demonstrates a loss of some key secondary structures. The phylogenetic analysis indicates an independent evolution of BpHyal when compared to other hyaluronidases. However, these toxins might share a common ancestor, thus suggesting a broad hyaluronidase-like distribution among venomous snakes.Conclusions This work is the first ... Article in Journal/Newspaper Arctic Directory of Open Access Journals: DOAJ Articles Arctic Journal of Venomous Animals and Toxins including Tropical Diseases 20 1 25 |
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Directory of Open Access Journals: DOAJ Articles |
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ftdoajarticles |
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English |
topic |
Alternative splicing Hyaluronidase-like Snake venom Arctic medicine. Tropical medicine RC955-962 Toxicology. Poisons RA1190-1270 Zoology QL1-991 |
spellingShingle |
Alternative splicing Hyaluronidase-like Snake venom Arctic medicine. Tropical medicine RC955-962 Toxicology. Poisons RA1190-1270 Zoology QL1-991 Letícia Eulalio Castanheira Renata Santos Rodrigues Johara Boldrini-França Fernando PP Fonseca Flávio Henrique-Silva Maria I Homsi-Brandeburgo Veridiana M Rodrigues Molecular cloning of a hyaluronidase fromBothrops pauloensisvenom gland |
topic_facet |
Alternative splicing Hyaluronidase-like Snake venom Arctic medicine. Tropical medicine RC955-962 Toxicology. Poisons RA1190-1270 Zoology QL1-991 |
description |
Background Hyaluronate is one of the major components of extracellular matrix from vertebrates whose breakdown is catalyzed by the enzyme hyaluronidase. These enzymes are widely described in snake venoms, in which they facilitate the spreading of the main toxins in the victim’s body during the envenoming. Snake venoms also present some variants (hyaluronidases-like substances) that are probably originated by alternative splicing, even though their relevance in envenomation is still under investigation. Hyaluronidases-like proteins have not yet been purified from any snake venom, but the cDNA that encodes these toxins was already identified in snake venom glands by transcriptomic analysis. Herein, we report the cloning and in silicoanalysis of the first hyaluronidase-like proteins from a Brazilian snake venom.Methods The cDNA sequence of hyaluronidase was cloned from the transcriptome of Bothrops pauloensisvenom glands. This sequence was submitted to multiple alignment with other related sequences by ClustalW. A phylogenetic analysis was performed using MEGA 4 software by the neighbor joining (NJ) method.Results The cDNA from Bothrops pauloensis venom gland that corresponds to hyaluronidase comprises 1175 bp and codifies a protein containing 194 amino acid residues. The sequence, denominated BpHyase, was identified as hyaluronidase-like since it shows high sequence identities (above 83%) with other described snake venom hyaluronidase-like sequences. Hyaluronidases-like proteins are thought to be products of alternative splicing implicated in deletions of central amino acids, including the catalytic residues. Structure-based sequence alignment of BpHyase to human hyaluronidase hHyal-1 demonstrates a loss of some key secondary structures. The phylogenetic analysis indicates an independent evolution of BpHyal when compared to other hyaluronidases. However, these toxins might share a common ancestor, thus suggesting a broad hyaluronidase-like distribution among venomous snakes.Conclusions This work is the first ... |
format |
Article in Journal/Newspaper |
author |
Letícia Eulalio Castanheira Renata Santos Rodrigues Johara Boldrini-França Fernando PP Fonseca Flávio Henrique-Silva Maria I Homsi-Brandeburgo Veridiana M Rodrigues |
author_facet |
Letícia Eulalio Castanheira Renata Santos Rodrigues Johara Boldrini-França Fernando PP Fonseca Flávio Henrique-Silva Maria I Homsi-Brandeburgo Veridiana M Rodrigues |
author_sort |
Letícia Eulalio Castanheira |
title |
Molecular cloning of a hyaluronidase fromBothrops pauloensisvenom gland |
title_short |
Molecular cloning of a hyaluronidase fromBothrops pauloensisvenom gland |
title_full |
Molecular cloning of a hyaluronidase fromBothrops pauloensisvenom gland |
title_fullStr |
Molecular cloning of a hyaluronidase fromBothrops pauloensisvenom gland |
title_full_unstemmed |
Molecular cloning of a hyaluronidase fromBothrops pauloensisvenom gland |
title_sort |
molecular cloning of a hyaluronidase frombothrops pauloensisvenom gland |
publisher |
SciELO |
publishDate |
2014 |
url |
https://doi.org/10.1186/1678-9199-20-25 https://doaj.org/article/f778258145b24e449da977a56a49f205 |
geographic |
Arctic |
geographic_facet |
Arctic |
genre |
Arctic |
genre_facet |
Arctic |
op_source |
Journal of Venomous Animals and Toxins including Tropical Diseases, Vol 20, Iss 0 (2014) |
op_relation |
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992014000200330&lng=en&tlng=en https://doaj.org/toc/1678-9199 1678-9199 doi:10.1186/1678-9199-20-25 https://doaj.org/article/f778258145b24e449da977a56a49f205 |
op_doi |
https://doi.org/10.1186/1678-9199-20-25 |
container_title |
Journal of Venomous Animals and Toxins including Tropical Diseases |
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20 |
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1 |
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25 |
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1766345782995189760 |