Autor(es): Lee, Kyeong Yong; Kim, Bo Yeon; Lee, Kwang Sik; Yoon, Hyung Joo; Jin, Byung Rae

Resumo: Serine protease inhibitors play a critical role in physiological processes and immune responses by regulating serine protease activities. Here we describe the molecular cloning and antimicrobial activities of a serine protease inhibitor from the hornfaced bee, Osmia cornifrons (OcSPI). OcSPI consists of 405 amino acid residues and contains a potential reactive center loop (RCL) region in its C-terminus. Recombinant OcSPI was produced as a 64-kDa glycoprotein in baculovirus-infected insect cells and exhibited inhibitory activity against chymotrypsin. Additionally, OcSPI demonstrated inhibitory activity against microbial serine proteases, such as subtilisin A and proteinase K, but not against tissue plasminogen activator, thrombin, or plasmin. Recombinant OcSPI bound directly to Escherichia coli, Bacillus subtilis, and Beauveria bassiana and exhibited antimicrobial activity against both bacteria and fungi. Our results demonstrated the antimicrobial functions of OcSPI and suggest a role for OcSPI in the immune response of O. cornifrons bees. (C) 2015 Korean Society of Applied Entomology, Taiwan Entomological Society and Malaysian Plant Protection Society. Published by Elsevier B.V. All rights reserved.

Palavras-Chave: Osmia cornifrons; Hornfaced bee; Serine protease inhibitor; Antimicrobial activity; Immune response

Imprenta: Journal of Asia-Pacific Entomology, v. 18, n. 3, p. 489-495, 2015

Identificador do objeto digital: 10.1016/j.aspen.2015.06.004

Descritores: Aedes aegypti - Immune response ; Aedes aegypti - Molecular structure

Data de publicação: 2015

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