Tight junction modulation and biochemical characterisation of the zonula occludens toxin C-and N-termini

E. Schmidt, S. M. Kelly, C. F. van der Walle

Research output: Contribution to journalArticle

25 Citations (Scopus)

Abstract

The ZOT N-terminal domain was expressed and refolded, yielding a soluble protein with defined secondary structure. Although distantly related to protein I of filamentous phages, no evidence of ATPase activity was found. It is therefore unlikely that the ZOT N-terminal domain is involved in cholera toxin phage packaging in Vibrio cholerae. The ZOT C-terminal domain caused delocalisation of occludin and ZO-1 from Caco-2 cell-cell contacts, irrespective of disulfide bridge formation in its putative binding domain. However, the C-terminal domain did not cause actin reorganisation and this may explain the absence of a concomitant reduction in the transepithelial electrical resistance across cell monolayers.

LanguageEnglish
Pages2974-2980
Number of pages7
JournalFEBS Letters
Volume581
Issue number16
DOIs
Publication statusPublished - 26 Jun 2007

Fingerprint

Bacteriophages
Tight Junctions
Modulation
Occludin
Acoustic impedance
Vibrio cholerae
Caco-2 Cells
Cholera Toxin
Product Packaging
Electric Impedance
Disulfides
Adenosine Triphosphatases
Actins
Monolayers
Packaging
Proteins
Vibrio cholerae zonula occludens toxin

Keywords

  • actins
  • Adenosine Triphosphatases
  • amino acid sequence
  • Caco-2 cells
  • cholera toxin
  • membrane proteins
  • molecular sequence data
  • occludin
  • phosphoproteins

Cite this

Schmidt, E. ; Kelly, S. M. ; van der Walle, C. F. / Tight junction modulation and biochemical characterisation of the zonula occludens toxin C-and N-termini. In: FEBS Letters. 2007 ; Vol. 581, No. 16. pp. 2974-2980.
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Tight junction modulation and biochemical characterisation of the zonula occludens toxin C-and N-termini. / Schmidt, E.; Kelly, S. M.; van der Walle, C. F.

In: FEBS Letters, Vol. 581, No. 16, 26.06.2007, p. 2974-2980.

Research output: Contribution to journalArticle

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AU - Schmidt, E.

AU - Kelly, S. M.

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AB - The ZOT N-terminal domain was expressed and refolded, yielding a soluble protein with defined secondary structure. Although distantly related to protein I of filamentous phages, no evidence of ATPase activity was found. It is therefore unlikely that the ZOT N-terminal domain is involved in cholera toxin phage packaging in Vibrio cholerae. The ZOT C-terminal domain caused delocalisation of occludin and ZO-1 from Caco-2 cell-cell contacts, irrespective of disulfide bridge formation in its putative binding domain. However, the C-terminal domain did not cause actin reorganisation and this may explain the absence of a concomitant reduction in the transepithelial electrical resistance across cell monolayers.

KW - actins

KW - Adenosine Triphosphatases

KW - amino acid sequence

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KW - cholera toxin

KW - membrane proteins

KW - molecular sequence data

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KW - phosphoproteins

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