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dc.contributor.authorLubker, Carolin
dc.contributor.authorDove, Stefan
dc.contributor.authorTang, Wei-Jen
dc.contributor.authorBieber Urbauer, Ramona J.
dc.contributor.authorMoskovitz, Jackob
dc.contributor.authorUrbauer, Jeffrey L.
dc.contributor.authorSeifert, Roland
dc.date.accessioned2016-02-12T21:41:21Z
dc.date.available2016-02-12T21:41:21Z
dc.date.issued2015-07-13
dc.identifier.citationLübker, Carolin, Stefan Dove, Wei-Jen Tang, Ramona Urbauer, Jackob Moskovitz, Jeffrey Urbauer, and Roland Seifert. "Different Roles of N-Terminal and C-Terminal Domains in Calmodulin for Activation of Bacillus Anthracis Edema Factor." Toxins 7.7 (2015): 2598-614. doi:10.3390/toxins7072598.en_US
dc.identifier.urihttp://hdl.handle.net/1808/20062
dc.description.abstractBacillus anthracis adenylyl cyclase toxin edema factor (EF) is one component of the anthrax toxin and is essential for establishing anthrax disease. EF activation by the eukaryotic Ca2+-sensor calmodulin (CaM) leads to massive cAMP production resulting in edema. cAMP also inhibits the nicotinamide adenine dinucleotide phosphate (NADPH)-oxidase, thus reducing production of reactive oxygen species (ROS) used for host defense in activated neutrophils and thereby facilitating bacterial growth. Methionine (Met) residues in CaM, important for interactions between CaM and its binding partners, can be oxidized by ROS. We investigated the impact of site-specific oxidation of Met in CaM on EF activation using thirteen CaM-mutants (CaM-mut) with Met to leucine (Leu) substitutions. EF activation shows high resistance to oxidative modifications in CaM. An intact structure in the C-terminal region of oxidized CaM is sufficient for major EF activation despite altered secondary structure in the N-terminal region associated with Met oxidation. The secondary structures of CaM-mut were determined and described in previous studies from our group. Thus, excess cAMP production and the associated impairment of host defence may be afforded even under oxidative conditions in activated neutrophils.en_US
dc.publisherMDPIen_US
dc.rightsThis article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/).
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/)
dc.subjectBacillus anthracis edema factoren_US
dc.subjectAdenylyl cyclase toxinen_US
dc.subject(Oxidized) calmodulinen_US
dc.subject(Oxidized) calmodulin mutantsen_US
dc.titleDifferent Roles of N-Terminal and C-Terminal Domains in Calmodulin for Activation of Bacillus anthracis Edema Factoren_US
dc.typeArticle
kusw.kuauthorMoskovitz, Jackob
kusw.kudepartmentPharmacology & Toxicologyen_US
dc.identifier.doi10.3390/toxins7072598
kusw.oaversionScholarly/refereed, publisher version
kusw.oapolicyThis item meets KU Open Access policy criteria.
dc.rights.accessrightsopenAccess


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This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/).
Except where otherwise noted, this item's license is described as: This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/).