A specific cathepsin-L-like protease purified from an insect midgut shows antibacterial activity against gut symbiotic bacteria. Issue 1 (November 2015)

• Record Type: Journal Article
• Authors: Byeon, Jin Hee; Seo, Eun Sil; Lee, Jun Beom; Lee, Min Ja; Kim, Jiyeun Kate; Yoo, Jin Wook; Jung, Yunjin; Lee, Bok Luel
• Is Part Of: Developmental and comparative immunology. Volume 53:Issue 1(2015)
• Page Start: 79
• Page End: 84
• Publication Date: 2015-11
• Subjects: Immunology -- Periodicals; Developmental immunology -- Periodicals; 616.079
• DOI: 10.1016/j.dci.2015.06.003
• Languages: English
• ISSNs: 0145-305X

Abstract

<abstract xml:lang="en" abstract-type="author" id="abs0010"> <title id="sectitle0010">Abstract</title> <sec> <p id="abspara0010">Because gut symbiotic bacteria affect host biology, host insects are expected to evolve some mechanisms for regulating symbiont population. The bean bug, <italic>Riptortus pedestris</italic>, harbors the <italic>Burkholderia</italic> 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 <italic>Burkholderia</italic> but not to cultured <italic>Burkholderia</italic>. However, the <italic>bona fide</italic> 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 <italic>Burkholderia</italic> but not the cultured <italic>Burkholderia.</italic> To further confirm this activity, recombinant cathepsin-L-like protease expressed in <italic>Escherichia coli</italic> also showed antibacterial activity against symbiotic <italic>Burkholderia</italic>. These results suggest that cathepsin-L-like protease purified from the M4B region plays a critical role in controlling the population of the <italic>Burkholderia</italic> gut symbiont.</p> </sec> </abstract>