标题:PslG, a self-produced glycosyl hydrolase, triggers biofilm disassembly by disrupting exopolysaccharide matrix
作者:Yu, Shan; Su, Tiantian; Wu, Huijun; Liu, Shiheng; Wang, Di; Zhao, Tianhu; Jin, Zengjun; Du, Wenbin; Zhu, Mei-Jun; Chua, Song Lin; 更多
作者机构:[Yu Shan] Institute of Microbiology, Chinese Academy of Sciences, State Key Laboratory of Microbial Resources, Beijing 100101, China.;[Wu Huijun] Inst 更多
通讯作者:Ma, LZ(luyanma27@im.ac.cn)
通讯作者地址:[Ma, LZ]Chinese Acad Sci, State Key Lab Microbial Resources, Inst Microbiol, Beijing 100101, Peoples R China.
来源:细胞研究
出版年:2015
卷:25
期:12
页码:1352-1367
DOI:10.1038/cr.2015.129
关键词:biofilm; glycosyl hydrolase; exopolysaccharide; PslG structure; biofilm; matrix; Pseudomonas
摘要:Biofilms are surface-associated communities of microorganism embedded in extracellular matrix. Exopolysaccharide is a critical component in the extracellular matrix that maintains biofilm architecture and protects resident biofilm bacteria from antimicrobials and host immune attack. However, self-produced factors that target the matrix exopolysaccharides, are still poorly understood. Here, we show that PslG, a protein involved in the synthesis of a key biofilm matrix exopolysaccharide Psl in Pseudomonas aeruginosa, prevents biofilm formation and disassembles existing biofilms within minutes at nanomolar concentrations when supplied exogenously. The crystal structure of PslG indicates the typical features of an endoglycosidase. PslG mainly disrupts the Psl matrix to disperse bacteria from biofilms. PslG treatment markedly enhances biofilm sensitivity to antibiotics and macrophage cells, resulting in improved biofilm clearance in a mouse implant infection model. Furthermore, PslG shows biofilm inhibition and disassembly activity against a wide range of Pseudomonas species, indicating its great potential in combating biofilm-related complications.
收录类别:CSCD;SCOPUS;SCIE
WOS核心被引频次:22
Scopus被引频次:22
资源类型:期刊论文
原文链接:https://www.scopus.com/inward/record.uri?eid=2-s2.0-84949095613&doi=10.1038%2fcr.2015.129&partnerID=40&md5=c1b8c7233522c7723a4695fc82adfe7f
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