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

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  • Additional Information
    • Source:
      Publisher: Academic Press Country of Publication: England NLM ID: 9505216 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1095-8274 (Electronic) Linking ISSN: 10759964 NLM ISO Abbreviation: Anaerobe Subsets: MEDLINE
    • Publication Information:
      Publication: London : Academic Press
      Original Publication: London ; San Diego : Academic Press, c1995-
    • Subject Terms:
      Bacterial Adhesion* ; Carrier Proteins*/chemistry ; Carrier Proteins*/immunology ; Carrier Proteins*/metabolism; Bacterial Outer Membrane Proteins/*metabolism ; Fusobacterium necrophorum/*metabolism; Animals ; Antibodies, Neutralizing ; Cattle ; Cell Line ; Fusobacterium Infections/metabolism ; Humans ; Immunoprecipitation ; Mass Spectrometry ; Recombinant Proteins/metabolism
    • Abstract:
      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.
      Competing Interests: Declaration of competing interest The authors declare that there are no conflicts of interest with respect to this manuscript.
      (Copyright © 2020 Elsevier Ltd. All rights reserved.)
    • Contributed Indexing:
      Keywords: 43 kDa outer membrane protein (43K OMP); BHK-21 cell; Bacterial adhesion; Fusobacterium necrophorum; Interaction proteins
    • Accession Number:
      0 (Antibodies, Neutralizing)
      0 (Bacterial Outer Membrane Proteins)
      0 (Carrier Proteins)
      0 (Recombinant Proteins)
    • Publication Date:
      Date Created: 20200406 Date Completed: 20210111 Latest Revision: 20210111
    • Publication Date:
      20240829
    • Accession Number:
      10.1016/j.anaerobe.2020.102184
    • Accession Number:
      32247918