4.6 Article

A specific cathepsin-L-like protease purified from an insect midgut shows antibacterial activity against gut symbiotic bacteria

Journal

DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY
Volume 53, Issue 1, Pages 79-84

Publisher

ELSEVIER SCI LTD
DOI: 10.1016/j.dci.2015.06.003

Keywords

Cathepsin L; Gut symbiosis; Riptortus pedestris; Burkholderia; Symbiont population

Funding

  1. Global Research Laboratory Program [2011-0021535]
  2. Basic Science Research Program of the National Research Foundation (NRF) of Korea [2014R1A1A4A01007507]
  3. National Research Foundation of Korea [2014R1A1A4A01007507] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)

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Because gut symbiotic bacteria affect host biology, host insects are expected to evolve some mechanisms for regulating symbiont population. The bean bug, Riptortus pedestris, harbors the Burkholderia genus as a gut symbiont in the midgut organ, designated as the M4 region. Recently, we demonstrated that the lysate of M4B, the region adjacent to M4, harbors potent antibacterial activity against symbiotic Burkholderia but not to cultured Burkholderia. However, the bona fide substance responsible for observed antibacterial activity was not identified in the previous study. Here, we report that cathepsin-L-like protease purified from the lysate of M4B showed strong antibacterial activity against symbiotic Burkholderia but not the cultured Burkholderia. To further confirm this activity, recombinant cathepsin-L-like protease expressed in Escherichia coli also showed antibacterial activity against symbiotic Burkholderia. These results suggest that cathepsin-L-like protease purified from the M4B region plays a critical role in controlling the population of the Burkholderia gut symbiont. (C) 2015 Elsevier Ltd. All rights reserved.

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