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Deletion Variants of Autotransporter from Psychrobacter cryohalolentis Increase Efficiency of 10 FN3 Exposure on the Surface of Escherichia coli Cells.

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  • معلومة اضافية
    • المصدر:
      Publisher: MAIK Nauka/Interperiodica Country of Publication: United States NLM ID: 0376536 Publication Model: Print Cited Medium: Internet ISSN: 1608-3040 (Electronic) Linking ISSN: 00062979 NLM ISO Abbreviation: Biochemistry (Mosc) Subsets: MEDLINE
    • بيانات النشر:
      Publication: <2007->: Moscow : MAIK Nauka/Interperiodica
      Original Publication: New York, Consultants Bureau [etc.]
    • الموضوع:
      Escherichia coli*/genetics ; Escherichia coli*/metabolism ; Type V Secretion Systems*/metabolism; 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine/analogs & derivatives ; Esterases/metabolism ; Fibronectins/metabolism ; Membrane Proteins/metabolism ; Psychrobacter
    • نبذة مختصرة :
      The autotransporter AT877 from Psychrobacter cryohalolentis belongs to the family of outer membrane proteins containing N-terminal passenger and C-terminal translocator domains that form the basis for the design of display systems on the surface of bacterial cells. It was shown in our previous study that the passenger domain of AT877 can be replaced by the cold-active esterase EstPc or the tenth domain of fibronectin type III ( 10 Fn3). In order to increase efficiency of the 10 Fn3 surface display in Escherichia coli cells, four deletion variants of the Fn877 hybrid autotransporter were obtained. It was demonstrated that all variants are present in the membrane of bacterial cells and facilitate binding of the antibodies specific against 10 Fn3 on the cell surface. The highest level of binding is provided by the variants Δ239 and Δ310, containing four and seven beta-strands out of twelve that comprise the structure of the translocator domain. Using electrophoresis under semi-native conditions, presence of heat modifiability in the full-size Fn877 and its deletion variants was demonstrated, which indicated preservation of beta structure in their molecules. The obtained results could be used to optimize the bacterial display systems of 10 Fn3, as well as of other heterologous passenger domains.
    • Contributed Indexing:
      Keywords: 10th human fibronectin type III domain; autotransporter; bacterial display; deletion variants; secretion
    • الرقم المعرف:
      0 (Fibronectins)
      0 (Membrane Proteins)
      0 (Type V Secretion Systems)
      84477-87-2 (1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine)
      EC 3.1.- (Esterases)
      Q0CH43PGXS (fasudil)
    • الموضوع:
      Psychrobacter cryohalolentis
    • الموضوع:
      Date Created: 20221001 Date Completed: 20221004 Latest Revision: 20221004
    • الموضوع:
      20240628
    • الرقم المعرف:
      10.1134/S0006297922090061
    • الرقم المعرف:
      36180989