Nuclear trafficking of the anti-apoptotic Coxiella burnetii effector protein AnkG requires binding to p32 and Importin-α1

Journal article
(Original article)


Publication Details

Author(s): Schäfer W, Eckart R, Schmid B, Cagköylü HA, Hof K, Muller Y, Amin B, Lührmann A
Journal: Cellular Microbiology
Publication year: 2016
Volume: 19
Journal issue: 1
ISSN: 1462-5822


Abstract


The obligate intracellular bacterium Coxiella burnetii causes the zoonotic disease Q-fever. Coxiella pathogenesis depends on a functional type IV secretion system (T4SS). The T4SS effector AnkG inhibits pathogen-induced host cell apoptosis, which is believed to be important for the establishment of a persistent infection. However, the mode of action of AnkG is not fully understood. We have previously demonstrated that binding of AnkG to p32 is crucial for migration of AnkG into the nucleus and that nuclear localization of AnkG is essential for its anti-apoptotic activity. Here, we compared the activity of AnkG from the C. burnetii strains Nine Mile and Dugway. Although there is only a single amino acid exchange at residue 11, we observed a difference in anti-apoptotic activity and nuclear migration. Mutation of amino acid 11 to glutamic acid, threonine or valine results in AnkG mutants that had lost the anti-apoptotic activity and the ability to migrate into the nucleus. We identified Importin-α1 to bind to AnkG, but not to the mutants and concluded that binding of AnkG to p32 and Importin-α1 is essential for migration into the nucleus. Also during Coxiella infection binding of AnkG to p32 and Importin-α1 is crucial for nuclear localization of AnkG.



FAU Authors / FAU Editors

Amin, Bushra Dr.
Sonderforschungsbereich 796 (mit integriertem Graduiertenkolleg) Steuerungsmechanismen mikrobieller Effektoren in Wirtszellen
Cagköylü, Hasret Askim
Sonderforschungsbereich 796 (mit integriertem Graduiertenkolleg) Steuerungsmechanismen mikrobieller Effektoren in Wirtszellen
Eckart, Rita
Lehrstuhl für Mikrobiologie
Muller, Yves Prof. Dr.
Lehrstuhl für Biotechnik (Proteinstruktur und -design)
Schmid, Benedikt Dr.
Lehrstuhl für Biotechnik (Proteinstruktur und -design)


How to cite

APA:
Schäfer, W., Eckart, R., Schmid, B., Cagköylü, H.A., Hof, K., Muller, Y.,... Lührmann, A. (2016). Nuclear trafficking of the anti-apoptotic Coxiella burnetii effector protein AnkG requires binding to p32 and Importin-α1. Cellular Microbiology, 19(1). https://dx.doi.org/10.1111/cmi.12634

MLA:
Schäfer, Walter, et al. "Nuclear trafficking of the anti-apoptotic Coxiella burnetii effector protein AnkG requires binding to p32 and Importin-α1." Cellular Microbiology 19.1 (2016).

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Last updated on 2018-19-04 at 03:40