Mutational analysis of the Helicobacter pylori vacuolating toxin amino terminus: Identification of amino acids essential for cellular vacuolation

Research output: Contribution to journalArticlepeer-review

Abstract

The functional importance of the amino terminus of the Helicobacter pylori vacuolating cytotoxin (VacA) was investigated by analyzing the relative levels of vacuolation of HeLa cells transfected with plasmids encoding wild-type and mutant forms of the toxin. Notably, VacA's intracellular activity was found to be sensitive to small truncations and internal deletions at the toxin's amino terminus. Moreover, alanine-scanning mutagenesis revealed the first VacA point mutations (at proline 9 or glycine 14) that completely abolish the toxin's intracellular activity.

Original languageEnglish (US)
Pages (from-to)4354-4357
Number of pages4
JournalInfection and immunity
Volume68
Issue number7
DOIs
StatePublished - Jul 2000

ASJC Scopus subject areas

  • Parasitology
  • Microbiology
  • Immunology
  • Infectious Diseases

Fingerprint Dive into the research topics of 'Mutational analysis of the Helicobacter pylori vacuolating toxin amino terminus: Identification of amino acids essential for cellular vacuolation'. Together they form a unique fingerprint.

Cite this