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

Authors
BURRONI D LUPETTI P PAGLIACCIA C REYRAT JM DALLAI R RAPPUOLI R TELFORD JL
Citation
D. Burroni et al., 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, Infection and immunity (Print), 66(11), 1998, pp. 5547-5550
Citations number
14
Categorie Soggetti
Immunology,"Infectious Diseases
Journal title
Infection and immunity (Print) → ACNP
ISSN journal
00199567
Volume
66
Issue
11
Year of publication
1998
Pages
5547 - 5550
Database
ISI
SICI code
0019-9567(1998)66:11<5547:DOTMPS>2.0.ZU;2-5
Abstract
The Helicobacter pylori cytotoxin is proteolytically cleaved at a flex ible hydrophilic loop into two subunits. Deletion of the loop sequence s had no effect on biological activity of the toxin in the HeLa cell v acuolation assay but favored the organization of the protein into hexa meric rather than heptameric structures.