title: Antarease-like Zn-metalloproteases are ubiquitous in the venom of different scorpion genera.
abstract: BACKGROUND
  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.
  
  
  METHODS
  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.
  
  
  RESULTS
  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.
  
  
  CONCLUSIONS
  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.
  
  
  CONCLUSIONS
  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.
authors.affiliation: Departamento de Medicina Molecular y Bioprocesos, Instituto de Biotecnología, Universidad Nacional Autonóma de México, Avenida Universidad 2001, Cuernavaca 62210, Mexico.
authors.forename: Ernesto
authors.initials: E
authors.lastname: Ortiz
authors.affiliation: Laboratorio Nacional de Genómica para la Biodiversidad, Centro de Investigación y de Estudios Avanzados del Instituto Politécnico Nacional, Km 9.6 Libramiento Norte Carretera León, Irapuato, Guanajuato 36821, Mexico.
authors.forename: Martha
authors.initials: M
authors.lastname: Rendón-Anaya
authors.affiliation: Departamento de Ciências Fisiológicas, Instituto de Ciências Biológicas, Universidade de Brasília, Brasília, DF 70910-900, Brazil.
authors.forename: Solange Cristina
authors.initials: SC
authors.lastname: Rego
authors.affiliation: Departamento de Ciências Fisiológicas, Instituto de Ciências Biológicas, Universidade de Brasília, Brasília, DF 70910-900, Brazil.
authors.forename: Elisabeth Ferroni
authors.initials: EF
authors.lastname: Schwartz
authors.affiliation: Departamento de Medicina Molecular y Bioprocesos, Instituto de Biotecnología, Universidad Nacional Autonóma de México, Avenida Universidad 2001, Cuernavaca 62210, Mexico. Electronic address: possani@ibt.unam.mx.
authors.forename: Lourival Domingos
authors.initials: LD
authors.lastname: Possani
mesh_terms: D000595:Amino Acid Sequence; D001483:Base Sequence; D045726:Metalloproteases / Q000737:chemistry* / Q000235:genetics / Q000502:physiology; D008958:Models, Molecular; D056004:Molecular Dynamics Simulation; D008969:Molecular Sequence Data; D058974:Phylogeography; D012604:Scorpion Venoms / Q000201:enzymology*
chemical_list: D012604:Scorpion Venoms; D045726:Metalloproteases
keywords: Antarease; Pancreatitis; Scorpion; Zn-metalloprotease; cDNA library