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Infection and Immunity, November 1998, p. 5547-5550, Vol. 66, No. 11
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Deletion of the Major Proteolytic Site of the Helicobacter pylori Cytotoxin Does Not Influence Toxin Activity but Favors Assembly of the Toxin into Hexameric Structures

Daniela Burroni,1 Pietro Lupetti,2 Cristina Pagliaccia,1 Jean Marc Reyrat,1 Romano Dallai,2 Rino Rappuoli,1 and John L. Telford1,*

IRIS, Chiron S.p.A.,1 and Dipartimento di Biologia Evolutiva, Università di Siena,2 53100 Siena, Italy

Received 3 June 1998/Returned for modification 24 July 1998/Accepted 18 August 1998

The Helicobacter pylori cytotoxin is proteolytically cleaved at a flexible hydrophilic loop into two subunits. Deletion of the loop sequences had no effect on biological activity of the toxin in the HeLa cell vacuolation assay but favored the organization of the protein into hexameric rather than heptameric structures.

* Corresponding author. Mailing address: IRIS, Chiron Spa, Via Fiorentina 1, 53100 Siena, Italy. Phone: 39 577 243470. Fax: 39 577 243564. E-mail: telford{at}iris02.biocine.it.

Infection and Immunity, November 1998, p. 5547-5550, Vol. 66, No. 11
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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