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Infection and Immunity, July 2000, p. 4354-4357, Vol. 68, No. 7
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Mutational Analysis of the Helicobacter pylori Vacuolating Toxin Amino Terminus: Identification of Amino Acids Essential for Cellular Vacuolation

Dan Ye and Steven R. Blanke*

Department of Biology and Biochemistry, University of Houston, Houston, Texas 77204-5513

Received 13 January 2000/Returned for modification 6 March 2000/Accepted 25 April 2000

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.

* Corresponding author. Mailing address: Department of Biology and Biochemistry, University of Houston, 430 Houston Science Center, 3201 Cullen Blvd., Houston, TX 77204-5513. Phone: (713) 743-8392. Fax: (713) 743-8351. E-mail: sblanke{at}uh.edu.

Infection and Immunity, July 2000, p. 4354-4357, Vol. 68, No. 7
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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