Autolysis at the disintegrin domain of patagonfibrase, a metalloproteinase from Philodryas patagoniensis (Patagonia Green Racer; Dipsadidae) venom

Autor(es)

Peichoto, Maria E. ^{[1, 2]} ; Paes Leme, Adriana F. ^[3] ; Pauletti, Bianca A. ^[3] ; Batista, Isabel Correia ^[4] ; Mackessy, Stephen P. ^[5] ; Acosta, Ofelia ^[2] ; Santoro, Marcelo L. ^[1]

Afiliação do(s) autor(es)

^[1] Inst Butantan, Lab Fisiopatol, BR-05503900 Sao Paulo - Brazil

^[2] Univ Nacl Nordeste, Catedra Farmacol, Fac Ciencias Vet, RA-3400 Corrientes - Argentina

^[3] CNPEM, Brazilian Biosci Natl Lab, LNBio Brazilian Ctr Res Energy & Mat, BR-13083970 Campinas, SP - Brazil

^[4] Inst Butantan, Lab Bioquim & Biofis, BR-05503900 Sao Paulo - Brazil

^[5] Univ No Colorado, Sch Biol Sci, Greeley, CO 80639 - USA

• Tipo de documento: Artigo Científico
• Fonte: BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS; v. 1804, n. 9, p. 1937-1942, SEP 2010.
• Citações Web of Science: 14

Resumo

Patagonfibrase is a 57.5-kDa hemorrhagic metalloproteinase isolated from the venom of Philodryas patagoniensis (Patagonia Green Racer), a South American rear-fanged snake. Herein we demonstrate that patagonfibrase undergoes autolysis at its pH optimum (7.5) and at 37 degrees C, primarily producing a similar to 32.6 kDa fragment composed of disintegrin-like and cysteine-rich domains, as identified by mass spectrometry and N-terminal sequencing. The autolysis site for production of this fragment is similar to that observed for metalloproteinases from front-fanged Viperidae snake venoms. In the presence of Ca(2+), patagonfibrase was only partially autolysed, giving rise mainly to one fragment of similar to 52.2 kDa. In addition, calcium markedly enhanced the azocaseinolytic activity of patagonfibrase. Our findings contribute to the understanding of the structural and mechanistic bases of this family of metalloenzymes that are widely distributed among snake venoms, demonstrating that important post-translational modifications such as proteolysis can also contribute to the diversity and complexity of proteins found in rear-fanged snake venoms. (C) 2010 Elsevier B.V. All rights reserved. (AU)

• Processo FAPESP: 08/02996-8 - Venenos de serpentes Bothrops jararaca recém-nascidas e adultas: comparação entre suas atividades enzimáticas e biológicas, imunoneutralização, composição química e capacidade de induzir alterações hemostáticas
• Beneficiário: Marcelo Larami Santoro
• Modalidade de apoio: Auxílio à Pesquisa - Regular