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. 2018 Apr 16;18:33. doi: 10.1186/s12866-018-1181-0

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© The Author(s). 2018

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Fig. 1 — Generation of a C. burnetii pldA mutant. a Alignment of PldA from E. coli and C. burnetii. The grey region shows the consensus sequence motif YTQ-X_n-G-X₂-H-X-SNG for PldA enzymes. Bold amino acids show known active site residues [15]. b Lysates from C. burnetii wild type, ΔpldA, and ΔpldAcomp strains after 6 days of growth in ACCM-2 (early SCV) were probed by immunoblotting with an anti-PldA polyclonal antibody