Screening of BHK-21 cellular proteins that interact with outer membrane protein 43K OMP of Fusobacterium necrophorum

被引：4

作者：

He, Xianjing ^{[1
]}

Wang, Lina ^{[1
]}

Li, He ^{[1
]}

Zhang, Siyao ^{[1
]}

Wang, Zhihui ^{[1
]}

Jiang, Jiancheng ^{[1
]}

Xiao, Jiawei ^{[1
]}

Wang, Fengfeng ^{[1
]}

Jiang, Kai ^{[1
]}

Zhao, Pengyu ^{[1
]}

Zhang, Aihui ^{[1
]}

Bi, Lan ^{[1
]}

Guo, Donghua ^{[1
]}

Sun, Dongbo ^{[1
]}

机构：

[1] Heilongjiang Bayi Agr Univ, Coll Anim Sci & Vet Med, Heilongjiang Prov Key Lab Prevent & Control Bovin, 5 Xinfeng Rd, Daqing 163319, Heilongjiang, Peoples R China

来源：

ANAEROBE | 2020年 / 63卷

基金：

中国国家自然科学基金;

关键词：

Fusobacterium necrophorum; 43 kDa outer membrane protein (43K OMP); Bacterial adhesion; BHK-21; cell; Interaction proteins; VIRULENCE FACTORS; NUCLEATUM; IDENTIFICATION; ARCHITECTURE; FIBRONECTIN; ADHERENCE; ENVELOPE; BINDING; FOMA;

D O I：

10.1016/j.anaerobe.2020.102184

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Fusobacterium necrophorum is a Gram negative, spore-free, anaerobic bacterium that can cause pyogenic and necrotic infections in animals and humans. It is a major bovine pathogen and causes hepatic abscesses, foot rot, and necrotic laryngitis. The 43K OMP of F. necrophorum is an outer membrane protein with molecular weight of 43 kDa, exhibiting similarity to pore-forming proteins of other Fusobacterium species that plays an important role in bacterial infections. However, the role of 43K OMP in F. necrophorum adhesion remains unknown. In this study, we evaluated whether the 43K OMP of F. necrophorum mediates adhesion to BHK-21 cells and performed a preliminary screen of the proteins that interact with 43K OMP of F. necrophorum by immunoprecipitation-mass spectrometry. The results showed that the natural 43K OMP and recombinant 43K OMP could bind to BHK-21 cells, and preincubation of F. necrophorum with an antibody against the recombinant 43K OMP of F. necrophorum decreased binding to BHK-21 cells. Seventy differential interacting proteins were successfully screened by immunoprecipitation-mass spectrometry. Among these seventy differential interacting proteins, seven cell membrane proteins and four extracellular matrix proteins shown to be relevant to bacteria adhesion through subcellular localization and single-molecule function analysis. These data increase our understanding of the pathogenesis of F. necrophorum and provide a new theoretical basis for the design of antimicrobial drugs against F. necrophorum. (C) 2020 Elsevier Ltd. All rights reserved.

引用

页数：6

共 23 条

[1] Stopping bacterial adhesion: A novel approach to treating infections [J].