Antarease-like Zn-metalloproteases are ubiquitous in the venom of different scorpion genera

The venoms of several scorpion species have long been associated with pancreatitis in animal models and humans. Antarease, a Zn-metalloprotease from Tityus serrulatus, is able to penetrate intact pancreatic tissue and disrupts the normal vesicular traffic necessary for secretion, so it could play a...

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Veröffentlicht in:Biochimica et biophysica acta Jg. 1840; H. 6; S. 1738 - 1746
Hauptverfasser: Ortiz, Ernesto, Rendón-Anaya, Martha, Rego, Solange Cristina, Schwartz, Elisabeth Ferroni, Possani, Lourival Domingos
Format: Journal Article
Sprache:Englisch
Veröffentlicht: Netherlands 01.06.2014
Schlagworte:
Amino Acid Sequence
animal models
antivenoms
Base Sequence
cDNA libraries
complementary DNA
humans
Metalloproteases - chemistry
Metalloproteases - genetics
Metalloproteases - physiology
metalloproteinases
Models, Molecular
molecular cloning
Molecular Dynamics Simulation
Molecular Sequence Data
pancreatitis
phylogeny
Phylogeography
physiological transport
polymerase chain reaction
Scorpion Venoms - enzymology
secretion
sequence analysis
Tityus serrulatus
venoms
Zn-metalloprotease
Scorpion
Antarease
Pancreatitis
cDNA library
ISSN:0304-4165, 0006-3002
Online-Zugang:Volltext
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Zusammenfassung:The venoms of several scorpion species have long been associated with pancreatitis in animal models and humans. Antarease, a Zn-metalloprotease from Tityus serrulatus, is able to penetrate intact pancreatic tissue and disrupts the normal vesicular traffic necessary for secretion, so it could play a relevant role in the onset of acute pancreatitis. The cDNA libraries from five different scorpion species were screened for antarease homologs with specific primers. The amplified PCR products were cloned and sequenced. A structural model was constructed to assess the functionality of the putative metalloproteases. A phylogenetic analysis was performed to identify clustering patterns of these venom components. Antarease-like sequences were amplified from all the screened cDNA libraries. The complete sequence of the antarease from T. serrulatus was obtained. The structural model of the putative antarease from Tityus trivittatus shows that it may adopt a catalytically active conformation, sharing relevant structural elements with previously reported metalloproteases of the ADAM family. The phylogenetic analysis reveals that the reported sequences cluster in groups that correlate with the geographical localization of the respective species. Antareases are ubiquitous to a broad range of scorpion species, where they could be catalytically active enzymes. These molecules can be used to describe the evolution of scorpion venoms under different ecogeographic constrains. For the first time the complete sequence of the antareases is reported. It is demonstrated that antareases are common in the venom of different scorpion species. They are now proposed as targets for antivenom therapies.
Bibliographie:ObjectType-Article-1
SourceType-Scholarly Journals-1
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ISSN:0304-4165
0006-3002
DOI:10.1016/j.bbagen.2013.12.012