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 journalArticlepeer-review

28 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.

Original languageEnglish
Pages (from-to)2974-2980
Number of pages7
JournalFEBS Letters
Volume581
Issue number16
DOIs
Publication statusPublished - 26 Jun 2007

Keywords

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

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