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Bactericidal Activity of Mouse α-Defensin, Cryptdin-4 Predominantly Affects Noncommensal Bacteria

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Title: Bactericidal Activity of Mouse α-Defensin, Cryptdin-4 Predominantly Affects Noncommensal Bacteria
Authors: Masuda, Koji Browse this author
Sakai, Naoki Browse this author
Nakamura, Kiminori Browse this author
Yoshioka, Sawako Browse this author
Ayabe, Tokiyoshi Browse this author
Keywords: Cryptdin-4
Bacteria, commensal, noncommensal
Disulfide bonds
Issue Date: Apr-2011
Publisher: Karger
Journal Title: Journal of Innate Immunity
Volume: 3
Issue: 3
Start Page: 315
End Page: 326
Publisher DOI: 10.1159/000322037
PMID: 21099205
Abstract: Mouse Paneth cell α-defensins, termed cryptdins, are secreted into the intestinal lumen, exert microbicidal activity and contribute to intestinal innate immunity. Among them, cryptdin-4 (Crp4) has the most potent microbicidal activity. In the intestinal lumen, commensal bacteria colonize and elicit beneficial effects to the host. However, the effects of Crp4 against commensal bacteria are poorly understood. Thus, we investigated the bactericidal activities of Crp4 against commensal bacteria compared to non-commensal bacteria. Oxidized Crp4 showed only minimal or no bactericidal activity against 8 out of 12 commensal bacterial species, including Bifidobacterium bifidum and Lactobacillus Casei. We further addressed a role of the conserved disulfide bonds of Crp4 by analyzing reduced Crp4 (r-Crp4). r-Crp4 demonstrated significantly greater bactericidal activities against 7 of 12 commensal bacteria than did oxidized Crp4. Oxidized Crp4 and r-Crp4 elicited equivalently potent bactericidal activities against 11 of 11 non-commensal bacteria tested such as Salmonella enterica serovar Typhimurium, and 5 of 12 commensal bacteria. Furthermore, when r-Crp4 was exposed to a processing enzyme of cryptdins, MMP-7, r-Crp4 was degraded and bactericidal activities disappeared. These findings suggest that Crp4 has selective bactericidal activities against intestinal microbiota and that the activities are dependent on the disulfide bonds.
Rights: Copyright © 2011 S. Karger AG, Basel
Type: article (author version)
Appears in Collections:生命科学院・先端生命科学研究院 (Graduate School of Life Science / Faculty of Advanced Life Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 綾部 時芳

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