Calpain-Mediated Processing of Adenylate Cyclase Toxin Generates a Cytosolic Soluble Catalytically Active N-Terminal Domain.
Bordetella pertussis, the whooping cough pathogen, secretes several virulence factors among which adenylate cyclase toxin (ACT) is essential for establishment of the disease in the respiratory tract. ACT weakens host defenses by suppressing important bactericidal activities of the phagocytic cells....
Main Authors: | Kepa B Uribe, Aitor Etxebarria, César Martín, Helena Ostolaza |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2013-01-01
|
Series: | PLoS ONE |
Online Access: | http://europepmc.org/articles/PMC3694075?pdf=render |
Similar Items
-
Understanding the Mechanism of Translocation of Adenylate Cyclase Toxin across Biological Membranes
by: Helena Ostolaza, et al.
Published: (2017-09-01) -
Adenylate cyclase toxin promotes internalisation of integrins and raft components and decreases macrophage adhesion capacity.
by: César Martín, et al.
Published: (2011-01-01) -
Ca2+ influx and tyrosine kinases trigger Bordetella adenylate cyclase toxin (ACT) endocytosis. Cell physiology and expression of the CD11b/CD18 integrin major determinants of the entry route.
by: Kepa B Uribe, et al.
Published: (2013-01-01) -
Membrane Permeabilization by <i>Bordetella</i> Adenylate Cyclase Toxin Involves Pores of Tunable Size
by: David González-Bullón, et al.
Published: (2019-05-01) -
Characterization of the Intrinsic Phospholipase A1 Activity of <i>Bordetella pertussis</i> Adenylate Cyclase Toxin
by: David González-Bullón, et al.
Published: (2018-12-01)