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Infection and Immunity, January 2001, p. 543-546, Vol. 69, No. 1
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.1.543-546.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Carboxy-Terminal Proteolytic Processing of Helicobacter pylori Vacuolating Toxin

Viet Q. Nguyen,1 Richard M. Caprioli,1 and Timothy L. Cover2,3,*

Mass Spectrometry Research Center1 and Departments of Medicine and Microbiology and Immunology,2 Vanderbilt University School of Medicine, and Veterans Affairs Medical Center,3 Nashville, Tennessee

Received 10 July 2000/Returned for modification 22 August 2000/Accepted 10 October 2000

The vacA gene of Helicobacter pylori strain 60190 encodes a 1,287-amino-acid protoxin, which undergoes cleavage of a 33-amino-acid amino-terminal signal sequence and carboxy-terminal proteolytic processing to yield a mature secreted toxin. Several features of VacA suggest that it belongs to the autotransporter family of gram-negative bacterial secreted proteins. Based on matrix-assisted laser desorption ionization-time of flight mass spectrometric analysis, we calculate that the mature toxin has a mass of 88.2 ± 0.2 kDa and consists of approximately 821 amino acids.

* Corresponding author. Mailing address: Division of Infectious Diseases, A3310 Medical Center North, Vanderbilt University School of Medicine, Nashville, TN 37232. Phone: (615) 322-2035. Fax: (615) 343-6160. E-mail: covertl{at}ctrvax.vanderbilt.edu.

Infection and Immunity, January 2001, p. 543-546, Vol. 69, No. 1
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.1.543-546.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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