BmSI-7, a novel subtilisin inhibitor from Boophilus microplus, with activity toward Pr1 proteases from the fungus Metarhizium anisopliae

BmSI-7, a novel subtilisin inhibitor from Boophilus microplus, with activity toward Pr1 proteases from the fungus Metarhizium anisopliae

Author Sasaki, Sergio D. Autor UNIFESP Google Scholar
Lima, Cdssia A. de Autor UNIFESP Google Scholar
Lovato, Diogo V. Autor UNIFESP Google Scholar
Juliano, Maria A. Autor UNIFESP Google Scholar
Torquato, Ricardo J. S. Autor UNIFESP Google Scholar
Tanaka, Aparecida S. Autor UNIFESP Google Scholar
Institution Universidade Federal de São Paulo (UNIFESP)
Abstract BmSI-7 and BmSI-6, two Boophilus microplus subtilisin inhibitors (BmSI) were purified and characterized from eggs. the inhibitors isolated by classical purification methods presented molecular masses of 7408 and 7271 Da, respectively, by MALDI-TOF-MS. Both BmSI-7 and BmSI-6 inhibited neutrophil elastase (K-i 0.4 and 0.3 nM) and subtilisin A (K-i 1.4 nM for both inhibitors). They also strongly inhibited Pr1 proteases from the fungus Metarhizium anisopliae; BmSI-7 (K-i 50 nM) and BmSI-6 (K-i 2.2 nM). the BmSI-7 full length cDNA was obtained using amino acid sequence information of BmSI-7 peptides generated by proteolytic digestion. BmSI-7 belongs to trypsin inhibitor like cysteine rich domain family (TIL), and it is transcribed in ovary, fat body, gut, salivary gland and haemocytes. BmSI-7 is the first TIL inhibitor described with inhibitory activity toward subtilisin A and Pr1 proteases of entomopathogenic fungi. (C) 2007 Elsevier Inc. All rights reserved.
Keywords Boophilus microplus
protease inhibitor
serine protease
egg proteins
tick
Metarhizium anisopliae protease
fungi
Language English
Date 2008-02-01
Published in Experimental Parasitology. San Diego: Academic Press Inc Elsevier Science, v. 118, n. 2, p. 214-220, 2008.
ISSN 0014-4894 (Sherpa/Romeo, impact factor)
Publisher Elsevier B.V.
Extent 214-220
Origin http://dx.doi.org/10.1016/j.exppara.2007.08.003
Access rights Closed access
Type Article
Web of Science ID WOS:000252982400010
URI http://repositorio.unifesp.br/handle/11600/30414

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