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-Reference-Cited by-同舟云学术

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

Published:1998-11 Issue:11 Volume:66 Page:5547-5550
ISSN:0019-9567
Container-title:Infection and Immunity
language:en
Short-container-title:Infect Immun

Author:

Burroni Daniela¹,Lupetti Pietro²,Pagliaccia Cristina¹,Reyrat Jean Marc¹,Dallai Romano²,Rappuoli Rino¹,Telford John L.¹

Affiliation:

1. IRIS, Chiron S.p.A.,1and

2. Dipartimento di Biologia Evolutiva, Università di Siena,2 53100 Siena, Italy

Abstract

ABSTRACT 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.

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Immunology,Microbiology,Parasitology

Link

https://journals.asm.org/doi/pdf/10.1128/IAI.66.11.5547-5550.1998

Reference14 articles.

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3. Protease susceptibility and toxicity of heat-labile enterotoxins with a mutation in the active site or in the protease-sensitive loop

4. Gene disruption and replacement as a feasible approach for mutagenesis of Campylobacter jejuni

5. Three dimensional reconstruction of metal replicas of the Helicobacter pylori vacuolating cytotoxin;Lanzavecchia S.;J. Struct. Biol.,1998

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