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Title: Boophilus microplus cathepsin L-like (BmCL1) cysteine protease: Specificity study using a peptide phage display library
Authors: Clara, Renan Orsati [UNIFESP]
Soares, Tatiane Sanches [UNIFESP]
Torquato, Ricardo Jose Soares [UNIFESP]
Lima, Cassia Arantes de [UNIFESP]
Watanabe, Renata Midori Okuta [UNIFESP]
Barros, Nilana Meza Tenório de [UNIFESP]
Carmona, Adriana Karaoglanovic [UNIFESP]
Masuda, Aoi
Vaz Junior, Itabajara S.
Tanaka, Aparecida Sadae [UNIFESP]
Universidade Federal de São Paulo (UNIFESP)
Univ Fed Rio Grande do Sul
Keywords: Cysteine proteases
Rhipicephalus (Boophilus) microplus
Protein expression
Enzyme kinetic
Phage display library
Issue Date: 27-Sep-2011
Publisher: Elsevier B.V.
Citation: Veterinary Parasitology. Amsterdam: Elsevier B.V., v. 181, n. 2-4, p. 291-300, 2011.
Abstract: The tick Rhipicephalus (Boophilus) microplus is one of the most important bovine ectoparasites, a disease vector responsible for losses in meat and milk productions. A cysteine protease similar to cathepsin L, named BmCL1, was previously identified in R. microplus gut, suggesting a role of the enzyme in meal digestion. in this work. BmCL1 was successfully expressed in Pichia pastoris system, yielding 54.8 mg/L of culture and its activity was analyzed by synthetic substrates and against a R. microplus cysteine protease inhibitor, Bmcystatin. After rBmCl1 biochemical characterization it was used in a selection of a peptide phage library to determine rBmCL1 substrate preference. Obtained sequenced clones showed that rBmCL1 has preference for Leu or Arg at P(1) position. the preference for Leu at position P(1) and the activation of BmCL1 after a Leu amino acid residue suggest possible self activation. (C) 2011 Elsevier B.V. All rights reserved.
ISSN: 0304-4017
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