HUSCAP logo Hokkaido Univ. logo

Hokkaido University Collection of Scholarly and Academic Papers >
Theses >
博士 (ソフトマター科学) >

Antimicrobial Properties and Mode of Action of Cryptdin-4, a Mouse α-Defensin Regulated by Peptide Redox Structures and Bacterial Cultivation Conditions

Files in This Item:
Yi_Wang.pdf1.07 MBPDFView/Open
Please use this identifier to cite or link to this item:https://doi.org/10.14943/doctoral.k15614
Related Items in HUSCAP:

Title: Antimicrobial Properties and Mode of Action of Cryptdin-4, a Mouse α-Defensin Regulated by Peptide Redox Structures and Bacterial Cultivation Conditions
Other Titles: マウス由来αディフェンシンCryptdin-4の酸化還元型構造と好気嫌気培養により制御される抗菌活性とメカニズム
Authors: 王, 一 Browse this author
Issue Date: 25-Sep-2023
Publisher: Hokkaido University
Abstract: Cryptdin-4 (crp4) is an enteric α-defensin derived from mice that is a main mediator of immunity to oral infections and a determinant of the composition of the intestinal microbiota. Structurally, crp4 exists in two states: the oxidized form (crp4oxi), constrained by three invariant disulfide bonds, and the reduced form (crp4red) with six free thiol groups, both of which exist in the intestinal tract. In this study, the antibacterial mechanisms of crp4 in both forms under aerobic and anaerobic conditions were investigated using Escherichia coli (E. coli), an anaerobic facultative bacterium, as a model. Fluorescent dye studies revealed that both crp4oxi and crp4red exhibited antimicrobial activity against cells cultured under aerobic conditions via rapid membrane depolarization. Furthermore, the antioxidant treatment experiments suggested that only crp4oxi exhibited antimicrobial activity by the induction and accumulation of reactive oxygen species (ROS). However, under anaerobic culture conditions, the ability of both forms to disrupt the function of bacterial membranes decreased, and activity was greatly reduced, but crp4red maintained some antimicrobial activity. This activity may be due to the inhibition of intracellular functions by DNA binding. Altogether, these data indicate that, according to its redox structure and the environmental redox conditions, crp4 could perform different antimicrobial activities via different mechanisms.
Conffering University: 北海道大学
Degree Report Number: 甲第15614号
Degree Level: 博士
Degree Discipline: ソフトマター科学
Examination Committee Members: (主査) 教授 相沢 智康, 教授 中村 公則, 教授 比能 洋
Degree Affiliation: 生命科学院(ソフトマター専攻)
Type: theses (doctoral)
URI: http://hdl.handle.net/2115/90805
Appears in Collections:課程博士 (Doctorate by way of Advanced Course) > 生命科学院(Graduate School of Life Science)
学位論文 (Theses) > 博士 (ソフトマター科学)

Export metadata:

OAI-PMH ( junii2 , jpcoar_1.0 )

MathJax is now OFF:


 

 - Hokkaido University