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. 2017 Jul 7;7:4879. doi: 10.1038/s41598-017-04853-9

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as 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 images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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R. solanacearum HpaB interacts with nine type III effectors. (a) Yeast cells were co-transformed by BD-HpaB and 38 AD-T3Es. Double transformation and interactions were tested by plating yeasts on synthetic dropout medium lacking leucine and tryptophan (SD/–Leu/–Trp) and synthetic dropout medium lacking leucine, tryptophan and histidine (SD/–Leu/–Trp/–His), respectively. RipW and RipG7 have the same profile as 26 other T3Es tested. BD-p53 and AD-T-antigen were used as negative controls. Three biological replicates were performed and gave same results. (b) Glutathione S-transferase (GST) and GST-T3Es were immobilized on glutathione sepharose and incubated with an E. coli lysate containing 6His-HpaB. Total cell lysates and eluted proteins were analyzed using antibodies directed against GST and the 6His epitope. Bands corresponding to GST and GST fusion proteins are marked by asterisks; lower bands represent degradation products. For lack of space, samples have been loaded into two gels (black line separation). The experiments have been repeated twice with similar results.